aspartic acid has been researched along with Brittle Bone Disease in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (10.00) | 18.7374 |
| 1990's | 7 (70.00) | 18.2507 |
| 2000's | 2 (20.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Galicka, A; Gindzieński, A; Wołczyński, S | 1 |
| Atkinson, M; Byers, PH; Culbert, AA; Kadler, KE; Lowe, MP; Wallis, GA | 1 |
| Cohen-Solal, L; Gomez Lira, M; Mottes, M; Sangalli, A; Zylberberg, L | 1 |
| Lund, AM; Raghunath, M; Schwartz, M; Skovby, F; Steinmann, B | 1 |
| Forlino, A; Keene, DR; Marini, JC; Schmidt, K | 1 |
| Atkinson, M; Byers, PH; Chitayat, D; Pace, JM; Schwarze, U; Wilcox, WR | 1 |
| Bonadio, J; Byers, PH; Eyre, DR; Niyibizi, C | 1 |
| Brass, A; Byers, PH; Grant, ME; Holmes, DF; Kadler, KE; Lightfoot, SJ | 1 |
| Constantinou, CD; Ganguly, A; Prockop, DJ; Zhuang, JP | 1 |
| Baldwin, CT; Constantinou, CD; Dumars, KW; Prockop, DJ | 1 |
10 other study(ies) available for aspartic acid and Brittle Bone Disease
| Article | Year |
|---|---|
Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta.
Topics: Aspartic Acid; Base Sequence; Cells, Cultured; Collagen Type I; Cyanogen Bromide; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Fibroblasts; Histidine; Humans; Infant; Osteogenesis Imperfecta; Peptide Fragments; Point Mutation; Procollagen; Proline; Skin; Trypsin; Twins | 2003 |
Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystall
Topics: Adult; Arginine; Aspartic Acid; Bone and Bones; Calcification, Physiologic; Collagen; Cyanogen Bromide; Durapatite; Electrophoresis, Polyacrylamide Gel; Female; Glycine; Heterozygote; Humans; Macromolecular Substances; Mutation; Osteogenesis Imperfecta; Peptide Mapping; Pregnancy; Procollagen; Protein Structure, Secondary | 1995 |
Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone.
Topics: Amino Acid Sequence; Aspartic Acid; Base Sequence; Bone and Bones; Calcification, Physiologic; Cells, Cultured; Collagen; DNA Primers; Female; Fetus; Fibroblasts; Gene Expression; Genes, Dominant; Genes, Lethal; Glycine; Humans; Infant; Male; Microscopy, Electron; Molecular Sequence Data; Osteogenesis Imperfecta; Point Mutation; Polymerase Chain Reaction; Pregnancy; Skin | 1994 |
Gly802Asp substitution in the pro alpha 2(I) collagen chain in a family with recurrent osteogenesis imperfecta due to paternal mosaicism.
Topics: Aspartic Acid; Base Sequence; Blotting, Southern; Cells, Cultured; Child; Collagen; DNA Primers; Electrophoresis, Polyacrylamide Gel; Fathers; Female; Glycine; Humans; Male; Molecular Sequence Data; Mosaicism; Mutation; Osteogenesis Imperfecta; Polymerase Chain Reaction; Procollagen; Temperature | 1996 |
An alpha2(I) glycine to aspartate substitution is responsible for the presence of a kink in type I collagen in a lethal case of osteogenesis imperfecta.
Topics: Amino Acid Substitution; Aspartic Acid; Collagen; Fatal Outcome; Glycine; Humans; Infant; Male; Osteogenesis Imperfecta | 1998 |
A single amino acid substitution (D1441Y) in the carboxyl-terminal propeptide of the proalpha1(I) chain of type I collagen results in a lethal variant of osteogenesis imperfecta with features of dense bone diseases.
Topics: Amino Acid Substitution; Aspartic Acid; Bone Density; Bone Diseases; Cell Line; Cells, Cultured; Collagen Type I; Female; Genes, Lethal; Humans; Infant, Newborn; Mutation; Osteogenesis Imperfecta; Peptide Fragments; Procollagen; Protein Processing, Post-Translational; Tyrosine | 2002 |
Incorporation of type I collagen molecules that contain a mutant alpha 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of osteogenesis imperfecta.
Topics: Amino Acid Sequence; Aspartic Acid; Base Sequence; Bone Matrix; Cloning, Molecular; Collagen; DNA; Genes, Lethal; Glycine; Humans; Infant; Macromolecular Substances; Molecular Sequence Data; Mutation; Oligodeoxyribonucleotides; Osteogenesis Imperfecta; Reference Values; RNA | 1992 |
Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule.
Topics: Amino Acid Sequence; Arginine; Aspartic Acid; Cells, Cultured; Collagen; Cysteine; Electrophoresis, Polyacrylamide Gel; Fibroblasts; Glycine; Humans; Kinetics; Macromolecular Substances; Microscopy, Electron; Mutation; Osteogenesis Imperfecta; Pepsin A; Procollagen; Procollagen N-Endopeptidase; Protein Processing, Post-Translational; Protein Structure, Secondary; Skin; Substrate Specificity; Trypsin | 1992 |
A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of prod
Topics: Adult; Aspartic Acid; Base Sequence; Carbodiimides; Cells, Cultured; Female; Fetal Death; Genes, Lethal; Glycine; Humans; Infant, Newborn; Infant, Premature; Male; Molecular Sequence Data; Mutation; Nucleic Acid Heteroduplexes; Nucleic Acid Hybridization; Osteogenesis Imperfecta; Polymerase Chain Reaction; Procollagen | 1991 |
A single base mutation that converts glycine 907 of the alpha 2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix.
Topics: Amino Acid Sequence; Aspartic Acid; Base Sequence; Cloning, Molecular; Female; Genes; Genes, Lethal; Genetic Variation; Glycine; Humans; Infant, Newborn; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Procollagen; Protein Conformation; Reference Values; Skin | 1989 |