Page last updated: 2024-08-17

methionine and Brittle Bone Disease

methionine has been researched along with Brittle Bone Disease in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Coucke, PJ; De Paepe, A; Legius, E; Malfait, F; Nuytinck, L; Symoens, S	1
Byers, PH; Chessler, SD; Wallis, GA	1

Other Studies

2 other study(ies) available for methionine and Brittle Bone Disease

Article	Year
Met>Val substitution in a highly conserved region of the pro-alpha1(I) collagen C-propeptide domain causes alternative splicing and a mild EDS/OI phenotype. Journal of medical genetics, 2004, Volume: 41, Issue:7 Topics: Alleles; Alternative Splicing; Amino Acid Substitution; Base Sequence; Child; Collagen; Collagen Type I; Collagen Type I, alpha 1 Chain; Conserved Sequence; Ehlers-Danlos Syndrome; Female; Fibroblasts; Humans; Methionine; Molecular Sequence Data; Osteogenesis Imperfecta; Peptide Fragments; Phenotype; Procollagen; Protein Precursors; RNA, Messenger; Skin; Valine	2004
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. The Journal of biological chemistry, 1993, Aug-25, Volume: 268, Issue:24 Topics: Amino Acid Sequence; Base Sequence; Cell Line; Cells, Cultured; Conserved Sequence; Disulfides; Female; Fetal Death; Fetus; Fibroblasts; Genes, Lethal; Humans; Infant, Newborn; Infant, Premature; Macromolecular Substances; Methionine; Molecular Sequence Data; Oligodeoxyribonucleotides; Osteogenesis Imperfecta; Point Mutation; Procollagen; Protein Structure, Secondary; Sequence Homology, Amino Acid; Skin	1993

Article

Year

Met>Val substitution in a highly conserved region of the pro-alpha1(I) collagen C-propeptide domain causes alternative splicing and a mild EDS/OI phenotype.

Journal of medical genetics, 2004, Volume: 41, Issue:7

Topics: Alleles; Alternative Splicing; Amino Acid Substitution; Base Sequence; Child; Collagen; Collagen Type I; Collagen Type I, alpha 1 Chain; Conserved Sequence; Ehlers-Danlos Syndrome; Female; Fibroblasts; Humans; Methionine; Molecular Sequence Data; Osteogenesis Imperfecta; Peptide Fragments; Phenotype; Procollagen; Protein Precursors; RNA, Messenger; Skin; Valine

2004

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.

The Journal of biological chemistry, 1993, Aug-25, Volume: 268, Issue:24

Topics: Amino Acid Sequence; Base Sequence; Cell Line; Cells, Cultured; Conserved Sequence; Disulfides; Female; Fetal Death; Fetus; Fibroblasts; Genes, Lethal; Humans; Infant, Newborn; Infant, Premature; Macromolecular Substances; Methionine; Molecular Sequence Data; Oligodeoxyribonucleotides; Osteogenesis Imperfecta; Point Mutation; Procollagen; Protein Structure, Secondary; Sequence Homology, Amino Acid; Skin

1993