serine has been researched along with Brittle Bone Disease in 19 studies
Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
serine : An alpha-amino acid that is alanine substituted at position 3 by a hydroxy group.
| Excerpt | Relevance | Reference |
|---|---|---|
| "Serine for glycine substitutions in type I collagen have been described in seven cases of lethal type II osteogenesis imperfecta (OI), and six cases of nonlethal OI." | 7.68 | Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology. ( Chen, KJ; Lewis, MB; Marini, JC; Orrison, BM; Wang, Q, 1993) |
| "Type I collagen alpha 1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI)." | 7.68 | Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity. ( Bateman, JF; Chan, D; Cole, WG; Hannagan, M; Moeller, I, 1992) |
| "Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier side chains for glycine residues and decreased the melting temperature of the triple helix." | 7.67 | Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid spe ( Constantinou, CD; Kalia, K; Nielsen, KB; Pack, M; Prockop, DJ, 1989) |
| "Serine for glycine substitutions in type I collagen have been described in seven cases of lethal type II osteogenesis imperfecta (OI), and six cases of nonlethal OI." | 3.68 | Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology. ( Chen, KJ; Lewis, MB; Marini, JC; Orrison, BM; Wang, Q, 1993) |
| "Type I collagen alpha 1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI)." | 3.68 | Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity. ( Bateman, JF; Chan, D; Cole, WG; Hannagan, M; Moeller, I, 1992) |
| "Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier side chains for glycine residues and decreased the melting temperature of the triple helix." | 3.67 | Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid spe ( Constantinou, CD; Kalia, K; Nielsen, KB; Pack, M; Prockop, DJ, 1989) |
| "In general, osteogenesis imperfecta (brittle bone disease) is caused by heterozygous mutations in the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively)." | 1.29 | A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III. ( Byers, PH; Dalgleish, R; Mackay, K; Rose, NJ, 1995) |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (10.53) | 18.7374 |
| 1990's | 13 (68.42) | 18.2507 |
| 2000's | 3 (15.79) | 29.6817 |
| 2010's | 1 (5.26) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Li, Y | 1 |
| Brodsky, B | 3 |
| Baum, J | 2 |
| Lee, KH | 1 |
| Holl, MM | 1 |
| Mooney, SD | 1 |
| Klein, TE | 1 |
| Galicka, A | 1 |
| Wołczyński, S | 1 |
| Gindzieński, A | 1 |
| Surazyński, A | 1 |
| Pałka, J | 1 |
| Mechelany-Leroy, L | 1 |
| Merckx, J | 1 |
| Rose, NJ | 2 |
| Mackay, K | 2 |
| Byers, PH | 2 |
| Dalgleish, R | 2 |
| Marini, JC | 2 |
| Lewis, MB | 2 |
| Wang, Q | 1 |
| Chen, KJ | 1 |
| Orrison, BM | 1 |
| Sztrolovics, R | 1 |
| Glorieux, FH | 1 |
| van der Rest, M | 1 |
| Roughley, PJ | 1 |
| Chen, K | 1 |
| Dyne, KM | 1 |
| Valli, M | 2 |
| Forlino, A | 1 |
| Mottes, M | 2 |
| Kresse, H | 1 |
| Cetta, G | 2 |
| Lund, AM | 1 |
| Skovby, F | 1 |
| Schwartz, M | 1 |
| Yang, W | 1 |
| Battineni, ML | 1 |
| Iida, T | 1 |
| Suzumori, K | 1 |
| Ikuta, K | 1 |
| Tanemura, M | 1 |
| Yagami, Y | 1 |
| Okamoto, T | 1 |
| Hata, A | 1 |
| Liu, X | 1 |
| Kim, S | 1 |
| Dai, QH | 1 |
| Bateman, JF | 1 |
| Moeller, I | 1 |
| Hannagan, M | 1 |
| Chan, D | 1 |
| Cole, WG | 1 |
| Sangalli, A | 1 |
| Gomez Lira, M | 1 |
| Tenni, R | 1 |
| Buttitta, P | 1 |
| Pignatti, PF | 1 |
| Westerhausen, A | 1 |
| Kishi, J | 1 |
| Prockop, DJ | 2 |
| Pack, M | 1 |
| Constantinou, CD | 1 |
| Kalia, K | 1 |
| Nielsen, KB | 1 |
| Trial | Phase | Enrollment | Study Type | Start Date | Status | ||
|---|---|---|---|---|---|---|---|
| Evaluation of Tomographic and Genetic Aspects of Keratoconus Patients Compared to Sounds Corneas[NCT03071302] | 210 participants (Actual) | Interventional | 2015-08-01 | Completed | |||
| [information is prepared from clinicaltrials.gov, extracted Sep-2024] | |||||||
1 review available for serine and Brittle Bone Disease
| Article | Year |
|---|---|
Deficient expression of the small proteoglycan decorin in a case of severe/lethal osteogenesis imperfecta.
Topics: Blotting, Northern; Blotting, Western; Cells, Cultured; Decorin; Extracellular Matrix Proteins; Fema | 1996 |
18 other studies available for serine and Brittle Bone Disease
| Article | Year |
|---|---|
NMR conformational and dynamic consequences of a gly to ser substitution in an osteogenesis imperfecta collagen model peptide.
Topics: Amino Acid Sequence; Amino Acid Substitution; Collagen; Glycine; Hydrogen; Magnetic Resonance Spectr | 2009 |
Free energy simulation to investigate the effect of amino acid sequence environment on the severity of osteogenesis imperfecta by glycine mutations in collagen.
Topics: Amino Acid Sequence; Amino Acid Substitution; Collagen Type I; Entropy; Extracellular Matrix; Genes, | 2011 |
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 Bon | 2002 |
Gly511 to Ser substitution in the COL1A1 gene in osteogenesis imperfecta type III patient with increased turnover of collagen.
Topics: Blotting, Western; Child, Preschool; Collagen; Collagen Type I; Collagen Type I, alpha 1 Chain; Cult | 2003 |
[Osteogenesis imperfecta with ketone hyperglycinemia, hyperserinemia and hyperornithinemia].
Topics: Child; Female; Glycine; Humans; Ornithine; Osteogenesis Imperfecta; Serine | 1980 |
A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III.
Topics: Base Sequence; Cells, Cultured; Child, Preschool; Collagen; Female; Glycine; Humans; Molecular Seque | 1995 |
A Gly859Ser substitution in the triple helical domain of the alpha 2 chain of type I collagen resulting in osteogenesis imperfecta type III in two unrelated individuals.
Topics: Adult; Base Sequence; Child, Preschool; Collagen; DNA Mutational Analysis; DNA Primers; DNA, Single- | 1994 |
Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology.
Topics: Amino Acid Sequence; Base Sequence; Child; Child, Preschool; Collagen; Cyanogen Bromide; Female; Gly | 1993 |
Identification of type I collagen gene (COL1A2) mutations in nonlethal osteogenesis imperfecta.
Topics: Amino Acid Sequence; Base Sequence; Cell Line; Codon; Collagen; Female; Fibroblasts; Glycine; Humans | 1993 |
Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen.
Topics: Child; Collagen; DNA Mutational Analysis; Female; Glycine; Humans; Osteogenesis Imperfecta; Point Mu | 1993 |
Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta.
Topics: Adolescent; Adult; Cells, Cultured; Child; Collagen; DNA Mutational Analysis; Exons; Fibroblasts; Ge | 1997 |
Amino acid sequence environment modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides.
Topics: Amino Acid Sequence; Circular Dichroism; Collagen; Glycine; Humans; Molecular Sequence Data; Osteoge | 1997 |
Identification of a Gly862 to Ser substitution in the type I collagen gene from a single spermatozoon.
Topics: Collagen; DNA; DNA Primers; Female; Fertilization in Vitro; Genetic Testing; Glycine; Humans; Male; | 1996 |
Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease.
Topics: Amino Acid Sequence; Amino Acid Substitution; Collagen; Glycine; Humans; Models, Molecular; Molecula | 1998 |
Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity.
Topics: Amino Acid Sequence; Base Sequence; Child; Collagen; Female; Glycine; Hot Temperature; Humans; Infan | 1992 |
Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene.
Topics: Base Sequence; Child; Chromosome Aberrations; Codon; Collagen; DNA Mutational Analysis; Female; Gene | 1992 |
Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blo
Topics: Base Sequence; Cells, Cultured; Codon; DNA; Fibroblasts; Glycine; Humans; Infant, Newborn; Infant, P | 1990 |
Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid spe
Topics: Cell Line; Cells, Cultured; Child, Preschool; Female; Fibroblasts; Gene Amplification; Genes; Geneti | 1989 |