arginine has been researched along with Brittle Bone Disease in 18 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 5 (27.78) | 18.7374 |
| 1990's | 9 (50.00) | 18.2507 |
| 2000's | 2 (11.11) | 29.6817 |
| 2010's | 2 (11.11) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Byers, PH; Chen, D; Espinoza, NA; Klein, TE; Leikin, S; Makareeva, E; Mertz, EL; Mirigian, LS; Sun, G; Vera, JC; Yang, K | 1 |
| Brodsky, B; Bryan, MA; Cheng, H | 1 |
| Chyczewski, L; Galicka, A; Gindzienski, A; Lesniewicz, R; Wolczynski, S | 1 |
| Atkinson, M; Byers, PH; Culbert, AA; Kadler, KE; Lowe, MP; Wallis, GA | 1 |
| Dalgleish, R; De Paepe, A; Mackay, K; Nuytinck, L | 1 |
| Bordenick, S; Chrousos, GP; Heavner, G; Hintz, R; Marini, JC; Rose, S; Rosenfeld, R | 1 |
| Cohen-Solal, L; Mottes, M; Pignatti, PF; Zolezzi, F | 1 |
| Cole, WG | 1 |
| Bank, RA; Janus, GJ; Pruijs, HE; Sakkers, RJ; Tekoppele, JM; Van der Sluijs, HA; Wassen, MH | 1 |
| Bateman, JF; Chan, D; Cole, WG; Hannagan, M; Moeller, I | 1 |
| Brass, A; Byers, PH; Grant, ME; Holmes, DF; Kadler, KE; Lightfoot, SJ | 1 |
| Amenta, PS; Constantinou, CD; Deak, SB; Gonzalez-Lavin, L; Levi-Minzi, SA; Mackenzie, JW; Scholz, PM | 1 |
| Byers, PH; Schwartz, MF; Starman, BJ; Wallis, GA | 1 |
| Bateman, J; Chan, D; Cole, W; Lamande, S; Mascara, T; Rogers, J | 1 |
| Baker, AT; Bateman, JF; Chan, D; Cole, WG; Ramshaw, JA | 1 |
| Byers, PH; Cohen, T; Cohn, DH; Wenstrup, RJ | 1 |
| Bateman, JF; Chan, D; Cole, WG; Rogers, JG; Walker, ID | 1 |
| Bateman, JF; Chan, D; Cole, WG; Dahl, HH; Lamande, SR | 1 |
18 other study(ies) available for arginine and Brittle Bone Disease
| Article | Year |
|---|---|
Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta.
Topics: Arginine; Circular Dichroism; Collagen Type I; Humans; Mutation; Osteogenesis Imperfecta; Procollagen; Protein Folding | 2018 |
Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Calorimetry, Differential Scanning; Circular Dichroism; Collagen Type I; Glycine; Humans; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Peptides; Protein Conformation; Protein Folding; Protein Stability; Protein Structure, Secondary; Protein Unfolding; Thermodynamics | 2011 |
A novel Gly to Arg substitution at position 388 of the alpha1 chain of type I collagen in lethal form of osteogenesis imperfecta.
Topics: Amino Acid Substitution; Arginine; Base Sequence; Collagen Type I; Genes, Lethal; Glycine; Hot Temperature; Humans; Male; Osteogenesis Imperfecta; Phenotype; Thermodynamics | 2002 |
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 glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III.
Topics: Alleles; Amino Acid Sequence; Arginine; Base Sequence; Collagen; Exons; Female; Glycine; Humans; Infant, Newborn; Male; Molecular Sequence Data; Osteogenesis Imperfecta; Point Mutation; Polymerase Chain Reaction; Reference Values; Restriction Mapping | 1994 |
The growth hormone and somatomedin axis in short children with osteogenesis imperfecta.
Topics: Adolescent; Arginine; Body Height; Child; Child, Preschool; Clonidine; Female; Growth Disorders; Growth Hormone; Humans; Insulin; Insulin-Like Growth Factor I; Levodopa; Male; Osteogenesis Imperfecta; Pilot Projects | 1993 |
Intrafamilial variable expressivity of osteogenesis imperfecta due to mosaicism for a lethal G382R substitution in the COL1A1 gene.
Topics: Arginine; Asparagine; Base Sequence; Collagen; Humans; Infant; Molecular Sequence Data; Mosaicism; Osteogenesis Imperfecta | 1996 |
The Nicholas Andry Award-1996. The molecular pathology of osteogenesis imperfecta.
Topics: 3T3 Cells; Animals; Arginine; Awards and Prizes; Bone and Bones; Cells, Cultured; Child; Collagen; Cysteine; Ehlers-Danlos Syndrome; Extracellular Matrix; Extracellular Matrix Proteins; Fibroblasts; Genotype; Glycine; Humans; Infant; Mice; Mice, Transgenic; Molecular Biology; Mutation; Osteogenesis Imperfecta; Phenotype; Point Mutation; Procollagen; Radiography; RNA; Skin | 1997 |
Pyridinium cross-links in bone of patients with osteogenesis imperfecta: evidence of a normal intrafibrillar collagen packing.
Topics: Adolescent; Adult; Amino Acids; Arginine; Biomarkers; Biopsy; Bone and Bones; Child; Child, Preschool; Collagen; Humans; Hydroxylysine; Infant; Lysine; Osteogenesis Imperfecta; Pepsin A; Pyridinium Compounds; Reference Values | 2000 |
Lethal perinatal osteogenesis imperfecta due to a type I collagen alpha 2(I) Gly to Arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatch.
Topics: Amino Acid Sequence; Arginine; Base Sequence; Cells, Cultured; Cloning, Molecular; Collagen; DNA; Electrophoresis, Polyacrylamide Gel; Female; Fibroblasts; Genes, Lethal; Glycine; Humans; Infant, Newborn; Male; Molecular Sequence Data; Nucleic Acid Heteroduplexes; Oligodeoxyribonucleotides; Osteogenesis Imperfecta; Peptide Fragments; Point Mutation; Polymerase Chain Reaction; RNA; RNA, Messenger | 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 |
The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.
Topics: Amino Acid Sequence; Arginine; Base Sequence; Blotting, Northern; Cells, Cultured; DNA; Fibroblasts; Glycine; Humans; Macromolecular Substances; Male; Middle Aged; Molecular Sequence Data; Mutation; Oligodeoxyribonucleotides; Osteogenesis Imperfecta; Peptide Mapping; Polymerase Chain Reaction; Procollagen; Protein Conformation; Protein Processing, Post-Translational; Reference Values; Restriction Mapping; RNA; Skin; Skin Physiological Phenomena; Thermodynamics | 1991 |
Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion.
Topics: Amino Acid Sequence; Arginine; Base Sequence; Cloning, Molecular; Collagen; Cyanogen Bromide; DNA; Glycine; Hot Temperature; Humans; Molecular Sequence Data; Mutation; Oligonucleotides; Osteogenesis Imperfecta; Peptide Mapping; Protein Conformation; Protein Denaturation | 1990 |
Correlation of clinical and molecular biological abnormalities in osteogenesis imperfecta.
Topics: Alanine; Arginine; Genotype; Glycine; Humans; Infant; Mutation; Osteogenesis Imperfecta; Phenotype; Valine | 1989 |
Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions.
Topics: Arginine; Collagen; Drug Stability; Glycine; Humans; Infant, Newborn; Models, Molecular; Mutation; Osteogenesis Imperfecta; Protein Conformation; Protein Denaturation | 1989 |
Arginine for glycine substitution in the triple-helical domain of the products of one alpha 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype.
Topics: Alleles; Arginine; Collagen; Deoxyribonuclease BamHI; DNA Restriction Enzymes; Glycine; Humans; Middle Aged; Osteogenesis Imperfecta; Pedigree; Phenotype; Polymorphism, Restriction Fragment Length; Protein Biosynthesis | 1988 |
Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the alpha 1(I) chain of type I collagen.
Topics: Amino Acid Sequence; Arginine; Bone and Bones; Collagen; Cyanogen Bromide; Electrophoresis, Polyacrylamide Gel; Female; Glycine; Humans; Hydroxylation; Infant, Newborn; Lysine; Mutation; Osteogenesis Imperfecta; Peptide Fragments; Procollagen; Trypsin | 1987 |
Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA.
Topics: Amino Acid Sequence; Arginine; Base Sequence; Collagen; DNA; DNA, Recombinant; Glycine; Humans; Infant, Newborn; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Protein Biosynthesis; Transcription, Genetic | 1988 |