cysteine has been researched along with Brittle Bone Disease in 36 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 10 (27.78) | 18.7374 |
| 1990's | 19 (52.78) | 18.2507 |
| 2000's | 6 (16.67) | 29.6817 |
| 2010's | 1 (2.78) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Fassier, F; Gaumond, MH; Jaiswal, PK; Moffatt, P; Patoine, A; Rauch, F | 1 |
| Klein, TE; Mooney, SD | 1 |
| Cabral, WA; Forlino, A; Kuznetsova, NV; Leikin, S; Marini, JC | 1 |
| Cabral, WA; Fertala, A; Keene, DR; Leikin, S; Letocha, AD; Makareeva, E; Marini, JC; Persikov, AV; Scribanu, N; Steplewski, A | 1 |
| Forlino, A; Kuznetsova, NV; Leikin, S; Marini, JC | 1 |
| Craig, D; Nicholls, AC; Pope, FM | 1 |
| Carnevale, E; Digilio, MC; Giannotti, A; Gomez-Lira, M; Mottes, M; Pignatti, PF; Sangalli, A | 1 |
| Akimoto, H; Hasegawa, T; Hattori, S; Hori, H; Kurosaka, D; Nagai, Y; Yamaguchi, N | 1 |
| Bruckner, P; Raghunath, M; Steinmann, B | 1 |
| de Vries, WN; de Wet, WJ; Glanville, RW; Hollister, DW; Labhard, ME; Pretorius, PJ; Rao, VH; Wirtz, MK | 1 |
| Fertala, A; Morris, G; Prockop, DJ; Rooney, JE; Westerhausen, A | 1 |
| Lever, LW; Phillips, CL; Quarles, LD; Wenstrup, RJ | 1 |
| Cole, WG | 1 |
| Forlino, A; Lee, EJ; Marini, JC; Porter, FD; Westphal, H | 1 |
| Brunoni, D; Cortelli, JR; Hart, PS; Hart, TC; Korkko, J; Pallos, D; Vian, S; Wright, JT | 1 |
| Byers, PH; Kuslich, CD; Pace, JM; Willing, MC | 1 |
| Byers, PH; Cohn, DH; Edwards, MJ; Wenstrup, RJ | 1 |
| Brass, A; Byers, PH; Grant, ME; Holmes, DF; Kadler, KE; Lightfoot, SJ | 1 |
| Adachi, E; Prockop, DJ; Romanic, AM; Torre-Blanco, A | 1 |
| Burn, VE; Burshell, AL; Chipman, SD; McKinstry, MB; Rowe, DW; Shapiro, JR; Stover, ML | 1 |
| Constantinou, CD; Prockop, DJ; Steinmann, B; Superti-Furga, A; Westerhausen, A | 1 |
| Antoniazzi, F; Cetta, G; Gomez Lira, M; Mottes, M; Pignatti, PF; Rossi, A; Sangalli, A; Tenni, R; Valli, M | 1 |
| Byers, PH; Cohn, DH; Lever, LW; Phillips, CL; Shrago-Howe, AW; Wenstrup, RJ | 1 |
| Adachi, E; Hojima, Y; Kadler, KE; Prockop, DJ; Torre-Blanco, A; Vogel, BE | 1 |
| Byers, PH; Cohn, DH | 1 |
| Constantinou, CD; Pack, M; Prockop, DJ; Young, SB | 1 |
| Cetta, G; Mottes, M; Pignatti, PF; Rossi, A; Tenni, R; Valli, M | 1 |
| Byers, PH; Charbonneau, H; Eyre, D; Graham, JM; Harrylock, M; Starman, BJ; Weis, MA; Weiss, L | 1 |
| Constantinou, CD; Nielsen, KB; Prockop, DJ | 1 |
| Royce, PM; Steinmann, B; Superti-Furga, A | 1 |
| Andreassen, P; Apone, S; Byers, PH; Charbonneau, H; Cohn, DH; Eyre, DR; Nicholls, AC; Pope, FM; Starman, BJ | 1 |
| Hollister, DW; Labhard, ME; Nicholls, AC; Pope, FM; Wirtz, MK | 1 |
| Hollister, DW | 1 |
| Freund, M; Minor, RR; Prockop, DJ; Vogel, BE | 1 |
| Nicholls, A; Pope, FM; Steinmann, B | 1 |
| de Vries, WN; de Wet, WJ | 1 |
1 review(s) available for cysteine and Brittle Bone Disease
| Article | Year |
|---|---|
Imperfect collagenesis in osteogenesis imperfecta. The consequences of cysteine-glycine substitutions upon collagen structure and metabolism.
Topics: Collagen; Cysteine; Glycine; Humans; Mutation; Osteogenesis Imperfecta | 1988 |
35 other study(ies) available for cysteine and Brittle Bone Disease
| Article | Year |
|---|---|
Topological mapping of BRIL reveals a type II orientation and effects of osteogenesis imperfecta mutations on its cellular destination.
Topics: Amino Acid Sequence; Animals; Cell Membrane; COP-Coated Vesicles; Cysteine; Endoplasmic Reticulum; Humans; Lipoylation; Membrane Proteins; Mice; Molecular Sequence Data; Mutant Proteins; Mutation; Osteogenesis Imperfecta; Protein Stability; Protein Transport; Structure-Activity Relationship | 2014 |
Structural models of osteogenesis imperfecta-associated variants in the COL1A1 gene.
Topics: Collagen Type I; Collagen Type I, alpha 1 Chain; Computer Simulation; Cysteine; Humans; Hydrogen Bonding; Models, Molecular; Mutation; Osteogenesis Imperfecta; Protein Structure, Tertiary; Serine; Valine | 2002 |
Structure, stability and interactions of type I collagen with GLY349-CYS substitution in alpha 1(I) chain in a murine Osteogenesis Imperfecta model.
Topics: Amino Acid Substitution; Animals; Collagen Type I; Cysteine; Disease Models, Animal; Enzyme Stability; Extracellular Matrix; Fibroblasts; Glycine; Mice; Osteogenesis Imperfecta; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Protein Structure, Quaternary; Tail; Tendons; Thermodynamics | 2004 |
Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype.
Topics: Adult; Amino Acid Sequence; Amino Acid Substitution; Cells, Cultured; Child; Collagen Type I; Cysteine; Dimerization; Ehlers-Danlos Syndrome; Humans; Infant; Male; Microscopy, Electron, Transmission; Mutation, Missense; Osteogenesis Imperfecta; Pedigree; Phenotype; Protein Structure, Tertiary; Sequence Analysis, Protein | 2007 |
Selective retention and degradation of molecules with a single mutant alpha1(I) chain in the Brtl IV mouse model of OI.
Topics: Animals; Cells, Cultured; Collagen Type I; Culture Media, Conditioned; Cysteine; Disease Models, Animal; Disulfides; Extracellular Space; Fibroblasts; Intracellular Space; Kinetics; Mice; Microscopy, Electron, Transmission; Mutation; Osteogenesis Imperfecta; Skin | 2007 |
An abnormal collagen alpha chain containing cysteine in autosomal dominant osteogenesis imperfecta.
Topics: Child; Collagen; Cysteine; Electrophoresis, Polyacrylamide Gel; Female; Genes, Dominant; Humans; Male; Osteogenesis Imperfecta | 1984 |
Determination of a new collagen type I alpha 2 gene point mutation which causes a Gly640 Cys substitution in osteogenesis imperfecta and prenatal diagnosis by DNA hybridisation.
Topics: Base Sequence; Collagen; Cysteine; DNA; Female; Glycine; Heterozygote; Humans; Molecular Sequence Data; Nucleic Acid Hybridization; Osteogenesis Imperfecta; Point Mutation; Pregnancy; Prenatal Diagnosis | 1994 |
Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta.
Topics: Base Sequence; Cells, Cultured; Cysteine; Disulfides; Glycine; Hot Temperature; Humans; Molecular Sequence Data; Osteogenesis Imperfecta; Point Mutation; Procollagen; RNA, Messenger | 1994 |
Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta.
Topics: Amino Acid Sequence; Cells, Cultured; Collagen; Cysteine; Fibroblasts; Glycine; Kinetics; Osteogenesis Imperfecta; Point Mutation; Procollagen; Protein Folding; Protein Structure, Secondary; Reference Values; Skin | 1994 |
A cysteine for glycine substitution at position 175 in an alpha 1 (I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta.
Topics: Amino Acid Sequence; Base Sequence; Chromatography, High Pressure Liquid; Collagen; Cysteine; DNA; Female; Fibroblasts; Glycine; Humans; Middle Aged; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Phenotype; Procollagen; Protein Processing, Post-Translational | 1993 |
Two cysteine substitutions in procollagen I: a glycine replacement near the N-terminus of alpha 1(I) chain causes lethal osteogenesis imperfecta and a glycine replacement in the alpha 2(I) chain markedly destabilizes the triple helix.
Topics: Base Sequence; Cells, Cultured; Cysteine; DNA; Fibroblasts; Genes, Lethal; Glycine; Humans; Infant, Newborn; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Procollagen; Protein Processing, Post-Translational; RNA, Messenger | 1993 |
Mutations in the COL1A2 gene of type I collagen that result in nonlethal forms of osteogenesis imperfecta.
Topics: Animals; Base Sequence; Bone and Bones; Cell Line; Cloning, Molecular; Collagen; Cysteine; DNA; Mice; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Peptide Mapping; Polymerase Chain Reaction; Procollagen; Temperature | 1993 |
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 |
Use of the Cre/lox recombination system to develop a non-lethal knock-in murine model for osteogenesis imperfecta with an alpha1(I) G349C substitution. Variability in phenotype in BrtlIV mice.
Topics: Alternative Splicing; Amino Acid Substitution; Animals; Base Sequence; Chimera; Collagen; Cysteine; Disease Models, Animal; Female; Glycine; Heterozygote; Humans; Integrases; Male; Mice; Mice, Mutant Strains; Molecular Sequence Data; Osteogenesis Imperfecta; Phenotype; RNA, Messenger; Viral Proteins | 1999 |
Novel COL1A1 mutation (G559C) [correction of G599C] associated with mild osteogenesis imperfecta and dentinogenesis imperfecta.
Topics: Amino Acid Substitution; Brazil; Chromosomes, Human, Pair 17; Collagen; Collagen Type I; Collagen Type I, alpha 1 Chain; Cysteine; Dentinogenesis Imperfecta; DNA Mutational Analysis; Female; Glycine; Humans; Joint Instability; Lod Score; Male; Mutation, Missense; Osteogenesis Imperfecta; Pedigree | 2001 |
Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proalpha1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfec
Topics: Amino Acid Sequence; Base Sequence; Collagen; Collagen Type I; Collagen Type I, alpha 1 Chain; Cysteine; Disulfides; Female; Fibroblasts; Humans; Infant, Newborn; Male; Molecular Sequence Data; Mutation, Missense; Osteogenesis Imperfecta; Pedigree; Peptide Fragments; Protein Precursors; Protein Structure, Quaternary; Protein Structure, Secondary; Radiography; Temperature | 2001 |
Recurrence of lethal osteogenesis imperfecta due to parental mosaicism for a mutation in the COL1A2 gene of type I collagen. The mosaic parent exhibits phenotypic features of a mild form of the disease.
Topics: Adult; Amino Acid Sequence; Base Sequence; Cells, Cultured; Collagen; Cysteine; DNA; Female; Fibroblasts; Genes, Lethal; Glycine; Humans; Infant, Newborn; Macromolecular Substances; Male; Molecular Sequence Data; Mosaicism; Mutation; Oligodeoxyribonucleotides; Osteogenesis Imperfecta; Pedigree; Phenotype; Polymerase Chain Reaction; Protein Denaturation; Sequence Homology, Amino Acid; Skin | 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 |
Copolymerization of normal type I collagen with three mutated type I collagens containing substitutions of cysteine at different glycine positions in the alpha 1 (I) chain.
Topics: Adult; Collagen; Cysteine; Electrophoresis, Polyacrylamide Gel; Fibroblasts; Glycine; Humans; Kinetics; Male; Mutation; Osteogenesis Imperfecta; Procollagen; Skin | 1992 |
An osteopenic nonfracture syndrome with features of mild osteogenesis imperfecta associated with the substitution of a cysteine for glycine at triple helix position 43 in the pro alpha 1(I) chain of type I collagen.
Topics: Adolescent; Adult; Base Sequence; Child; Child, Preschool; Collagen; Cysteine; DNA; Electrophoresis, Polyacrylamide Gel; Female; Glycine; Humans; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Osteoporosis; Protein Conformation | 1992 |
Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(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.
Topics: Alleles; Base Sequence; Cells, Cultured; Cysteine; Female; Fibroblasts; Glycine; Humans; Infant, Newborn; Molecular Sequence Data; Mutation; Nucleic Acid Hybridization; Osteogenesis Imperfecta; Prenatal Diagnosis; Procollagen; Protein Conformation; Skin | 1991 |
A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain.
Topics: Alleles; Amino Acid Sequence; Base Sequence; Blotting, Northern; Collagen; Cysteine; Glycine; Hot Temperature; Humans; Male; Molecular Sequence Data; Oligonucleotide Probes; Osteogenesis Imperfecta; Peptide Mapping; Protein Denaturation | 1991 |
The effects of different cysteine for glycine substitutions within alpha 2(I) chains. Evidence of distinct structural domains within the type I collagen triple helix.
Topics: Amino Acid Sequence; Base Sequence; Cells, Cultured; Child; Cloning, Molecular; Cysteine; Female; Glycine; Heterozygote; Humans; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Procollagen; Protein Conformation; Protein Denaturation; Temperature | 1991 |
A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures.
Topics: Cells, Cultured; Collagen; Cysteine; Electrophoresis, Polyacrylamide Gel; Fibroblasts; Glycine; Humans; Kinetics; Macromolecular Substances; Models, Structural; Mutation; Osteogenesis Imperfecta; Procollagen; Protein Conformation; Reference Values; Skin | 1991 |
Cysteine in the triple helical domain of the pro alpha 2(I) chain of type-I collagen in nonlethal forms of osteogenesis imperfecta.
Topics: Adult; Child; Collagen; Cysteine; Electrophoresis, Polyacrylamide Gel; Female; Humans; Infant, Newborn; Male; Molecular Structure; Mutation; Osteogenesis Imperfecta; Pedigree | 1991 |
Phenotypic heterogeneity in osteogenesis imperfecta: the mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for alpha 1-glycine 904 in a type I procollagen gene (COL1A1).
Topics: Alleles; Base Sequence; Blotting, Southern; Cysteine; DNA; DNA Mutational Analysis; Female; Fetal Death; Fibroblasts; Genes, Lethal; Glycine; Humans; Leukocyte Count; Male; Molecular Sequence Data; Mosaicism; Mutation; Osteogenesis Imperfecta; Pedigree; Polymerase Chain Reaction; Procollagen; Protein Processing, Post-Translational | 1990 |
Anomalous cysteine in type I collagen. Localisation by chemical cleavage of the protein using 2-nitro-5-thiocyanobenzoic acid and by mismatch analysis of cDNA heteroduplexes.
Topics: Base Sequence; Collagen; Cysteine; DNA; Fibroblasts; Humans; Molecular Sequence Data; Nucleic Acid Hybridization; Osteogenesis Imperfecta; Polymerase Chain Reaction; Skin; Thiocyanates | 1990 |
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.
Topics: Adult; Amino Acid Sequence; Child; Child, Preschool; Chromatography, DEAE-Cellulose; Collagen; Cysteine; Electrophoresis, Polyacrylamide Gel; Female; Glycine; Humans; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Peptides; Phenotype | 1989 |
A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable typ
Topics: Base Sequence; Cysteine; Female; Fetal Death; Genes, Lethal; Glycine; Humans; Infant, Newborn; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Peptide Mapping; Pregnancy; Procollagen | 1989 |
Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta.
Topics: Alleles; Amino Acid Sequence; Base Sequence; Cells, Cultured; Collagen; Cysteine; Fibroblasts; Gene Amplification; Genes; Glycine; Humans; Molecular Sequence Data; Mutation; Osteogenesis Imperfecta; Peptide Fragments; Skin | 1988 |
A cysteine for glycine substitution at position 1017 in an alpha 1(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta.
Topics: Adolescent; Amino Acid Sequence; Base Sequence; Cloning, Molecular; Collagen; Cysteine; Glycine; Humans; Male; Mutation; Osteogenesis Imperfecta; Peptide Fragments | 1988 |
Molecular basis of osteogenesis imperfecta.
Topics: Amino Acid Sequence; Base Sequence; Collagen; Cysteine; DNA; Fibroblasts; Humans; Hydroxylysine; Infant; Infant, Newborn; Male; Osteogenesis Imperfecta; Phenotype; Polymorphism, Genetic; Proteins | 1987 |
A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta.
Topics: Amino Acid Sequence; Base Sequence; Cloning, Molecular; Cysteine; Disulfides; DNA; Glycine; Hot Temperature; Humans; Male; Mutation; Osteogenesis Imperfecta; Peptides; Procollagen; Protein Conformation | 1987 |
Clinical variability of osteogenesis imperfecta reflecting molecular heterogeneity: cysteine substitutions in the alpha 1(I) collagen chain producing lethal and mild forms.
Topics: Adolescent; Collagen; Cyanogen Bromide; Cysteine; Genetic Variation; Humans; Male; Osteogenesis Imperfecta; Peptide Fragments; Skin | 1986 |
The molecular defect in an autosomal dominant form of osteogenesis imperfecta. Synthesis of type I procollagen containing cysteine in the triple-helical domain of pro-alpha 1(I) chains.
Topics: Chymotrypsin; Cyanogen Bromide; Cysteine; Disulfides; Fibroblasts; Genes, Dominant; Humans; Kinetics; Macromolecular Substances; Osteogenesis Imperfecta; Peptide Fragments; Procollagen; Protein Conformation; Skin; Trypsin | 1986 |