serine has been researched along with Osteogenesis Imperfecta 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.
Osteogenesis Imperfecta: COLLAGEN DISEASES characterized by brittle, osteoporotic, and easily fractured bones. It may also present with blue sclerae, loose joints, and imperfect dentin formation. Most types are autosomal dominant and are associated with mutations in COLLAGEN TYPE I.
| 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 Osteogenesis Imperfecta
| 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 Osteogenesis Imperfecta
| 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 |