glycine has been researched along with Brittle Bone Disease in 106 studies
| Excerpt | Relevance | Reference |
|---|---|---|
| "Osteogenesis imperfecta (OI) is a disease caused primarily by mutations of glycine in the standard (Xaa-Yaa-Gly)n repeat of a type I collagen triple helix." | 7.83 | Synthetic, Register-Specific, AAB Heterotrimers to Investigate Single Point Glycine Mutations in Osteogenesis Imperfecta. ( Acevedo-Jake, AM; Clements, KA; Hartgerink, JD, 2016) |
| "Pamidronate treatment in children with all types of OI increased LS BMD, decreased fracture rate, and improved vertebral compression fractures." | 7.83 | Decreased fracture rate, pharmacogenetics and BMD response in 79 Swedish children with osteogenesis imperfecta types I, III and IV treated with Pamidronate. ( Åström, E; Grigelioniene, G; Kindmark, A; Lindahl, K; Ljunggren, Ö; Malmgren, B; Rubin, CJ; Söderhäll, S, 2016) |
| "Osteogenesis imperfecta (OI), or brittle bone disease, often results from missense mutation of one of the conserved glycine residues present in the repeating Gly-X-Y sequence characterizing the triple-helical region of type I collagen." | 7.74 | Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations. ( Bodian, DL; Brodsky, B; Klein, TE; Madhan, B, 2008) |
| "We identified two infants with lethal (type II) osteogenesis imperfecta (OI) who were heterozygous for mutations in the COL1A1 gene that resulted in substitutions of aspartic acid for glycine at position 220 and arginine for glycine at position 664 in the product of one COL1A1 allele in each individual." | 7.69 | 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 ( Atkinson, M; Byers, PH; Culbert, AA; Kadler, KE; Lowe, MP; Wallis, GA, 1995) |
| "The features of a child with osteogenesis imperfecta type III (OI III) resulting from the heterozygous substitution of glycine 1006 by alanine in the pro alpha 2(I) chain of type I procollagen were studied." | 7.69 | Arachnoid cyst and chronic subdural haematoma in a child with osteogenesis imperfecta type III resulting from the substitution of glycine 1006 by alanine in the pro alpha 2(I) chain of type I procollagen. ( Cole, WG; Lam, TP, 1996) |
| "The skeleton of a child with osteogenesis imperfecta type III, resulting from the substitution of glycine 586 by valine in the triple helical domain of the alpha 2 (I) chain of type I collagen, was severely porotic but contained lamellar bone and Haversian systems." | 7.69 | Disrupted growth plates and progressive deformities in osteogenesis imperfecta as a result of the substitution of glycine 585 by valine in the alpha 2 (I) chain of type I collagen. ( Bateman, JF; Chan, D; Chow, CW; Cole, WG; Rogers, JG, 1996) |
| "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) |
| "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) |
| "A proband with a lethal variant of osteogenesis imperfecta (OI) has been shown to have, in one allele in a gene for type I procollagen (COL1A1), a single base mutation that converted the codon for alpha 1-glycine 904 to a codon for cysteine." | 7.68 | 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). ( Constantinou, CD; Pack, M; Prockop, DJ; Young, SB, 1990) |
| "Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer." | 7.68 | 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. ( Antoniazzi, F; Cetta, G; Gomez Lira, M; Mottes, M; Pignatti, PF; Rossi, A; Sangalli, A; Tenni, R; Valli, M, 1991) |
| "Skin fibroblasts from a proband with lethal osteogenesis imperfecta synthesized a type I procollagen containing a cysteine residue in the alpha 1(I) helical domain." | 7.68 | 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. ( Constantinou, CD; Prockop, DJ; Steinmann, B; Superti-Furga, A; Westerhausen, A, 1991) |
| "Two substitutions for glycine in the triple-helical domain were found in type I procollagen synthesized by skin fibroblasts from two probands with lethal osteogenesis imperfecta." | 7.68 | Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. ( Constantinou, CD; Prockop, DJ; Tsuneyoshi, T; Westerhausen, A, 1991) |
| "The features of three babies with perinatal lethal osteogenesis imperfecta (OI II) resulting from substitutions of glycine by valine in the triple helical domain of the alpha 1(I) chain of type I collagen were studied." | 7.68 | The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen. ( Bonadio, J; Campbell, PE; Cole, WG; Fortune, DW; Patterson, E, 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) |
| "Skin fibroblasts grown from three individuals with osteogenesis imperfecta (OI) each synthesized a population of normal type I collagen molecules and additional molecules that had one or two alpha 1(I) chains that contained a cysteine residue within the triple-helical domain, a region from which cysteine normally is excluded." | 7.67 | 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. ( Byers, PH; Charbonneau, H; Eyre, D; Graham, JM; Harrylock, M; Starman, BJ; Weis, MA; Weiss, L, 1989) |
| "The effect of glycine-to-arginine mutations in the alpha 1 (I)-chain on collagen triple-helix structure in lethal perinatal osteogenesis imperfecta was studied by determination of the helix denaturation temperature and by computerized molecular modelling." | 7.67 | Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions. ( Baker, AT; Bateman, JF; Chan, D; Cole, WG; Ramshaw, JA, 1989) |
| "Perinatal lethal osteogenesis imperfecta is the result of heterozygous mutations of the COL1A1 and COL1A2 genes." | 5.30 | Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes. Mutations in brief no. 152. Online. ( Freising, P; Gomez Lira, M; Lisi, V; Mottes, M; Valli, M; Zolezzi, F, 1998) |
| "Osteogenesis imperfecta(OI) is a disease caused by substitution in glycine residues with different amino acids in type I collagen (Gly-Xaa-Yaa)n." | 4.12 | Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy. ( Lu, C; Qiang, S; Xu, F, 2022) |
| "Osteogenesis imperfecta (OI) is a disease caused primarily by mutations of glycine in the standard (Xaa-Yaa-Gly)n repeat of a type I collagen triple helix." | 3.83 | Synthetic, Register-Specific, AAB Heterotrimers to Investigate Single Point Glycine Mutations in Osteogenesis Imperfecta. ( Acevedo-Jake, AM; Clements, KA; Hartgerink, JD, 2016) |
| "Pamidronate treatment in children with all types of OI increased LS BMD, decreased fracture rate, and improved vertebral compression fractures." | 3.83 | Decreased fracture rate, pharmacogenetics and BMD response in 79 Swedish children with osteogenesis imperfecta types I, III and IV treated with Pamidronate. ( Åström, E; Grigelioniene, G; Kindmark, A; Lindahl, K; Ljunggren, Ö; Malmgren, B; Rubin, CJ; Söderhäll, S, 2016) |
| "Osteogenesis imperfecta (OI), or brittle bone disease, often results from missense mutation of one of the conserved glycine residues present in the repeating Gly-X-Y sequence characterizing the triple-helical region of type I collagen." | 3.74 | Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations. ( Bodian, DL; Brodsky, B; Klein, TE; Madhan, B, 2008) |
| "The majority of osteogenesis imperfecta (OI) is caused by substitutions for glycine residues in the two alpha chains of type I collagen." | 3.71 | G76E substitution in type I collagen is the first nonlethal glutamic acid substitution in the alpha1(I) chain and alters folding of the N-terminal end of the helix. ( Cabral, WA; Chernoff, EJ; Marini, JC, 2001) |
| "We identified two infants with lethal (type II) osteogenesis imperfecta (OI) who were heterozygous for mutations in the COL1A1 gene that resulted in substitutions of aspartic acid for glycine at position 220 and arginine for glycine at position 664 in the product of one COL1A1 allele in each individual." | 3.69 | 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 ( Atkinson, M; Byers, PH; Culbert, AA; Kadler, KE; Lowe, MP; Wallis, GA, 1995) |
| "The skeleton of a child with osteogenesis imperfecta type III, resulting from the substitution of glycine 586 by valine in the triple helical domain of the alpha 2 (I) chain of type I collagen, was severely porotic but contained lamellar bone and Haversian systems." | 3.69 | Disrupted growth plates and progressive deformities in osteogenesis imperfecta as a result of the substitution of glycine 585 by valine in the alpha 2 (I) chain of type I collagen. ( Bateman, JF; Chan, D; Chow, CW; Cole, WG; Rogers, JG, 1996) |
| "The features of a child with osteogenesis imperfecta type III (OI III) resulting from the heterozygous substitution of glycine 1006 by alanine in the pro alpha 2(I) chain of type I procollagen were studied." | 3.69 | Arachnoid cyst and chronic subdural haematoma in a child with osteogenesis imperfecta type III resulting from the substitution of glycine 1006 by alanine in the pro alpha 2(I) chain of type I procollagen. ( Cole, WG; Lam, TP, 1996) |
| "Previous observations with type I collagen from a proband with lethal osteogenesis imperfecta demonstrated that type I collagen containing a substitution of cysteine for glycine alpha 1-748 copolymerized with normal type I collagen (Kadler, K." | 3.68 | 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. ( Adachi, E; Prockop, DJ; Romanic, AM; Torre-Blanco, A, 1992) |
| "The features of three babies with perinatal lethal osteogenesis imperfecta (OI II) resulting from substitutions of glycine by valine in the triple helical domain of the alpha 1(I) chain of type I collagen were studied." | 3.68 | The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen. ( Bonadio, J; Campbell, PE; Cole, WG; Fortune, DW; Patterson, E, 1992) |
| "Two substitutions for glycine in the triple-helical domain were found in type I procollagen synthesized by skin fibroblasts from two probands with lethal osteogenesis imperfecta." | 3.68 | Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. ( Constantinou, CD; Prockop, DJ; Tsuneyoshi, T; Westerhausen, A, 1991) |
| "Skin fibroblasts from a proband with lethal osteogenesis imperfecta synthesized a type I procollagen containing a cysteine residue in the alpha 1(I) helical domain." | 3.68 | 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. ( Constantinou, CD; Prockop, DJ; Steinmann, B; Superti-Furga, A; Westerhausen, A, 1991) |
| "Cultured fibroblasts from a patient affected with a moderate form of osteogenesis imperfecta were defective for the synthesis of type I collagen molecules; about half of the alpha 1(I) chains contained a cysteine residue in the triple helical domain and a disulfide link formed when two mutant alpha 1(I) chains were incorporated into a type I collagen heterotrimer." | 3.68 | 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. ( Antoniazzi, F; Cetta, G; Gomez Lira, M; Mottes, M; Pignatti, PF; Rossi, A; Sangalli, A; Tenni, R; Valli, M, 1991) |
| "Affected individuals from two apparently distinct, mild osteogenesis imperfecta families were heterozygous for a G to T transition in the COL1A2 gene that resulted in cysteine for glycine substitutions at position 646 in the alpha 2(I) chain of type I collagen." | 3.68 | 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. ( Byers, PH; Cohn, DH; Lever, LW; Phillips, CL; Shrago-Howe, AW; Wenstrup, RJ, 1991) |
| "A proband with a lethal variant of osteogenesis imperfecta (OI) has been shown to have, in one allele in a gene for type I procollagen (COL1A1), a single base mutation that converted the codon for alpha 1-glycine 904 to a codon for cysteine." | 3.68 | 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). ( Constantinou, CD; Pack, M; Prockop, DJ; Young, SB, 1990) |
| "In this paper we describe a mild moderate form of osteogenesis imperfecta caused by a point mutation in COL1A1 which converted glycine 85 to valine." | 3.68 | Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion. ( Antoniazzi, F; Cetta, G; Mottes, M; Pignatti, P; Stanzial, F; Tenni, R; Valli, M; Zolezzi, F, 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) |
| "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) |
| "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) |
| "Substitution of a glycine residue in the triple helix of the alpha 1(I) chain by either arginine, valine or alanine was associated with the type II lethal perinatal osteogenesis imperfecta phenotype." | 3.67 | Correlation of clinical and molecular biological abnormalities in osteogenesis imperfecta. ( Bateman, J; Chan, D; Cole, W; Lamande, S; Mascara, T; Rogers, J, 1989) |
| "The effect of glycine-to-arginine mutations in the alpha 1 (I)-chain on collagen triple-helix structure in lethal perinatal osteogenesis imperfecta was studied by determination of the helix denaturation temperature and by computerized molecular modelling." | 3.67 | Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions. ( Baker, AT; Bateman, JF; Chan, D; Cole, WG; Ramshaw, JA, 1989) |
| "Skin fibroblasts grown from three individuals with osteogenesis imperfecta (OI) each synthesized a population of normal type I collagen molecules and additional molecules that had one or two alpha 1(I) chains that contained a cysteine residue within the triple-helical domain, a region from which cysteine normally is excluded." | 3.67 | 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. ( Byers, PH; Charbonneau, H; Eyre, D; Graham, JM; Harrylock, M; Starman, BJ; Weis, MA; Weiss, L, 1989) |
| "Perinatal lethal osteogenesis imperfecta is the result of heterozygous mutations of the COL1A1 and COL1A2 genes." | 1.30 | Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes. Mutations in brief no. 152. Online. ( Freising, P; Gomez Lira, M; Lisi, V; Mottes, M; Valli, M; Zolezzi, F, 1998) |
| "The mild form of osteogenesis imperfecta is caused by quantitative anomalies of Type I collagen." | 1.30 | The Nicholas Andry Award-1996. The molecular pathology of osteogenesis imperfecta. ( Cole, WG, 1997) |
| "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 | 17 (16.04) | 18.7374 |
| 1990's | 56 (52.83) | 18.2507 |
| 2000's | 17 (16.04) | 29.6817 |
| 2010's | 12 (11.32) | 24.3611 |
| 2020's | 4 (3.77) | 2.80 |
| Authors | Studies |
|---|---|
| Shi, H | 1 |
| Zhao, L | 1 |
| Zhai, C | 1 |
| Yeo, J | 1 |
| Garibaldi, N | 1 |
| Besio, R | 1 |
| Dalgleish, R | 6 |
| Villani, S | 1 |
| Barnes, AM | 1 |
| Marini, JC | 10 |
| Forlino, A | 8 |
| Sałacińska, K | 1 |
| Michałus, I | 1 |
| Pinkier, I | 1 |
| Rutkowska, L | 1 |
| Chlebna-Sokół, D | 1 |
| Jakubowska-Pietkiewicz, E | 1 |
| Kępczyński, Ł | 1 |
| Salachna, D | 1 |
| Gach, A | 1 |
| Qiang, S | 1 |
| Lu, C | 1 |
| Xu, F | 1 |
| Sun, X | 1 |
| Yao, L | 2 |
| Fu, C | 1 |
| Luo, L | 2 |
| Wang, J | 2 |
| Xiao, J | 4 |
| Qiu, Y | 1 |
| Mekkat, A | 1 |
| Yu, H | 1 |
| Yigit, S | 1 |
| Hamaia, S | 1 |
| Farndale, RW | 1 |
| Kaplan, DL | 2 |
| Lin, YS | 1 |
| Brodsky, B | 9 |
| Liu, Z | 1 |
| Yu, J | 1 |
| Takagi, M | 1 |
| Shinohara, H | 1 |
| Narumi, S | 1 |
| Nishimura, G | 1 |
| Hasegawa, Y | 1 |
| Hasegawa, T | 2 |
| Acevedo-Jake, AM | 1 |
| Clements, KA | 1 |
| Hartgerink, JD | 1 |
| Lindahl, K | 1 |
| Kindmark, A | 1 |
| Rubin, CJ | 1 |
| Malmgren, B | 1 |
| Grigelioniene, G | 1 |
| Söderhäll, S | 1 |
| Ljunggren, Ö | 1 |
| Åström, E | 1 |
| Hruskova, L | 1 |
| Fijalkowski, I | 1 |
| Van Hul, W | 1 |
| Marik, I | 1 |
| Mortier, G | 1 |
| Martasek, P | 1 |
| Mazura, I | 1 |
| Gautieri, A | 2 |
| Vesentini, S | 2 |
| Redaelli, A | 2 |
| Buehler, MJ | 2 |
| Faqeih, E | 1 |
| Roughley, P | 1 |
| Glorieux, FH | 2 |
| Rauch, F | 1 |
| Li, Y | 2 |
| Baum, J | 4 |
| Uzel, S | 1 |
| Bryan, MA | 1 |
| Cheng, H | 2 |
| Lee, KH | 1 |
| Holl, MM | 1 |
| Madhan, B | 2 |
| Silva, T | 1 |
| Chen, CP | 1 |
| Lin, SP | 1 |
| Suo, YN | 1 |
| Chern, SR | 1 |
| Su, JW | 1 |
| Wang, W | 1 |
| Galicka, A | 2 |
| Wolczynski, S | 1 |
| Lesniewicz, R | 1 |
| Chyczewski, L | 1 |
| Gindzienski, A | 2 |
| Wołczyński, S | 1 |
| Surazyński, A | 1 |
| Pałka, J | 1 |
| Radmer, RJ | 1 |
| Klein, TE | 2 |
| Kuznetsova, NV | 1 |
| Cabral, WA | 4 |
| Leikin, S | 1 |
| Milgrom, S | 1 |
| Letocha, AD | 1 |
| Moriarty, E | 1 |
| Bodian, DL | 1 |
| Krane, SM | 1 |
| Xu, P | 1 |
| Huang, J | 1 |
| Cebe, P | 1 |
| Mechelany-Leroy, L | 1 |
| Merckx, J | 1 |
| Culbert, AA | 1 |
| Lowe, MP | 1 |
| Atkinson, M | 1 |
| Byers, PH | 13 |
| Wallis, GA | 2 |
| Kadler, KE | 4 |
| Valli, M | 7 |
| Sangalli, A | 5 |
| Rossi, A | 2 |
| Mottes, M | 9 |
| Tenni, R | 4 |
| Pignatti, PF | 5 |
| Cetta, G | 6 |
| Wang, Q | 2 |
| Orrison, BM | 2 |
| Lu, J | 1 |
| Costa, T | 1 |
| Cole, WG | 11 |
| Rose, NJ | 3 |
| Mackay, K | 5 |
| Zolezzi, F | 3 |
| Brunelli, PC | 1 |
| Gomez-Lira, M | 1 |
| Digilio, MC | 1 |
| Giannotti, A | 1 |
| Carnevale, E | 1 |
| Kurosaka, D | 1 |
| Hattori, S | 1 |
| Hori, H | 1 |
| Yamaguchi, N | 1 |
| Akimoto, H | 1 |
| Nagai, Y | 1 |
| Lightfoot, SJ | 2 |
| Atkinson, MS | 1 |
| Murphy, G | 1 |
| De Paepe, A | 2 |
| Nuytinck, L | 2 |
| Lewis, MB | 2 |
| Chen, KJ | 1 |
| Lund, AM | 3 |
| Raghunath, M | 3 |
| Steinmann, B | 5 |
| Bruckner, P | 1 |
| Cohen-Solal, L | 2 |
| Zylberberg, L | 1 |
| Gomez Lira, M | 4 |
| Antoniazzi, F | 2 |
| Stanzial, F | 1 |
| Pignatti, P | 1 |
| Wirtz, MK | 2 |
| Rao, VH | 1 |
| Glanville, RW | 1 |
| Labhard, ME | 2 |
| Pretorius, PJ | 1 |
| de Vries, WN | 1 |
| de Wet, WJ | 1 |
| Hollister, DW | 2 |
| Sztrolovics, R | 1 |
| van der Rest, M | 1 |
| Roughley, PJ | 1 |
| Fertala, A | 1 |
| Westerhausen, A | 4 |
| Morris, G | 1 |
| Rooney, JE | 1 |
| Prockop, DJ | 12 |
| Chen, K | 1 |
| Dyne, KM | 1 |
| Kresse, H | 1 |
| Lam, TP | 1 |
| Schwartz, M | 2 |
| Skovby, F | 2 |
| Chan, D | 8 |
| Chow, CW | 1 |
| Rogers, JG | 2 |
| Bateman, JF | 7 |
| 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 |
| Sarafova, AP | 1 |
| Choi, H | 1 |
| Gajko, A | 1 |
| Tosi, L | 1 |
| Reing, CM | 1 |
| Liu, X | 1 |
| Kim, S | 1 |
| Dai, QH | 1 |
| Keene, DR | 1 |
| Schmidt, K | 1 |
| Porter, FD | 1 |
| Lee, EJ | 1 |
| Westphal, H | 1 |
| Lisi, V | 1 |
| Freising, P | 1 |
| Beck, K | 1 |
| Chan, VC | 1 |
| Shenoy, N | 1 |
| Kirkpatrick, A | 1 |
| Ramshaw, JA | 2 |
| Tükel, T | 1 |
| Kayserili, H | 1 |
| Apak, MY | 1 |
| Campbell, BG | 1 |
| Wootton, JA | 1 |
| MacLeod, JN | 1 |
| Minor, RR | 2 |
| Chernoff, EJ | 1 |
| Pallos, D | 1 |
| Hart, PS | 1 |
| Cortelli, JR | 1 |
| Vian, S | 1 |
| Wright, JT | 1 |
| Korkko, J | 1 |
| Brunoni, D | 1 |
| Hart, TC | 1 |
| Müller, PK | 1 |
| Lemmen, C | 1 |
| Gay, S | 1 |
| Meigel, WN | 1 |
| Moeller, I | 2 |
| Hannagan, M | 3 |
| Edwards, MJ | 1 |
| Wenstrup, RJ | 3 |
| Cohn, DH | 4 |
| Niyibizi, C | 1 |
| Bonadio, J | 2 |
| Eyre, DR | 2 |
| Holmes, DF | 1 |
| Brass, A | 1 |
| Grant, ME | 1 |
| Bonaventure, J | 1 |
| Lasselin, C | 1 |
| Maroteaux, P | 1 |
| Torre-Blanco, A | 2 |
| Adachi, E | 2 |
| Romanic, AM | 1 |
| Patterson, E | 1 |
| Campbell, PE | 1 |
| Fortune, DW | 1 |
| Buttitta, P | 1 |
| Deak, SB | 1 |
| Scholz, PM | 1 |
| Amenta, PS | 1 |
| Constantinou, CD | 8 |
| Levi-Minzi, SA | 1 |
| Gonzalez-Lavin, L | 1 |
| Mackenzie, JW | 1 |
| Shapiro, JR | 1 |
| Stover, ML | 1 |
| Burn, VE | 1 |
| McKinstry, MB | 1 |
| Burshell, AL | 1 |
| Chipman, SD | 1 |
| Rowe, DW | 1 |
| Tsuneyoshi, T | 1 |
| Superti-Furga, A | 2 |
| Shrago-Howe, AW | 1 |
| Lever, LW | 1 |
| Phillips, CL | 1 |
| Zhuang, JP | 1 |
| Ganguly, A | 1 |
| Vogel, BE | 2 |
| Hojima, Y | 1 |
| Kishi, J | 1 |
| Starman, BJ | 3 |
| Schwartz, MF | 1 |
| Pack, M | 2 |
| Young, SB | 1 |
| Sykes, B | 1 |
| Kalia, K | 1 |
| Nielsen, KB | 2 |
| Cole, W | 1 |
| Lamande, S | 1 |
| Mascara, T | 1 |
| Rogers, J | 1 |
| Bateman, J | 1 |
| Baker, AT | 1 |
| Eyre, D | 1 |
| Charbonneau, H | 2 |
| Harrylock, M | 1 |
| Weis, MA | 1 |
| Weiss, L | 1 |
| Graham, JM | 1 |
| Cohen, T | 1 |
| Baldwin, CT | 1 |
| Dumars, KW | 1 |
| Royce, PM | 1 |
| Gage, JP | 1 |
| Francis, MJ | 1 |
| Whitaker, GE | 1 |
| Smith, R | 1 |
| Walker, ID | 1 |
| Apone, S | 1 |
| Andreassen, P | 1 |
| Nicholls, AC | 2 |
| Pope, FM | 2 |
| Lamande, SR | 1 |
| Dahl, HH | 1 |
| Freund, M | 1 |
| Eastoe, JE | 1 |
| Martens, P | 1 |
| Thomas, NR | 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] | |||||||
3 reviews available for glycine and Brittle Bone Disease
| Article | Year |
|---|---|
The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens.
Topics: Amino Acid Sequence; Animals; Collagen; Glycine; Humans; Hydroxyproline; Mice; Models, Biological; M | 2008 |
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 |
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 |
103 other studies available for glycine and Brittle Bone Disease
| Article | Year |
|---|---|
Specific osteogenesis imperfecta-related Gly substitutions in type I collagen induce distinct structural, mechanical, and dynamic characteristics.
Topics: Collagen Type I; Glycine; Humans; Markov Chains; Molecular Conformation; Molecular Dynamics Simulati | 2021 |
Dissecting the phenotypic variability of osteogenesis imperfecta.
Topics: Animals; Biological Variation, Population; Collagen; Collagen Type I, alpha 1 Chain; Glycine; Humans | 2022 |
The first glycine-to-tryptophan substitution in the COL1A1 gene identified in a patient with progressively-deforming Osteogenesis imperfecta.
Topics: Collagen Type I; Collagen Type I, alpha 1 Chain; Glycine; Humans; Osteogenesis Imperfecta; Tryptopha | 2022 |
Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.
Topics: Amino Acid Substitution; Circular Dichroism; Collagen; Glycine; Humans; Hydrogen Bonding; Mutation; | 2022 |
Detection of target collagen peptides with single amino acid mutation using two fluorescent peptide probes.
Topics: Amino Acid Sequence; Amino Acid Substitution; Collagen; Fluorescence; Fluorescent Dyes; Glycine; Hum | 2019 |
Collagen Gly missense mutations: Effect of residue identity on collagen structure and integrin binding.
Topics: Amino Acid Sequence; Amino Acid Substitution; Circular Dichroism; Collagen Type I; Glycine; Humans; | 2018 |
Morphology of Osteogenesis Imperfecta Collagen Mimetic Peptide Assemblies Correlates with the Identity of Glycine-Substituting Residue.
Topics: Amino Acid Sequence; Collagen; Glycine; Models, Molecular; Osteogenesis Imperfecta; Peptidomimetics; | 2019 |
Severe osteogenesis imperfecta caused by double glycine substitutions near the amino-terminal triple helical region in COL1A2.
Topics: Amino Acid Substitution; Base Sequence; Collagen Type I; DNA Mutational Analysis; Female; Glycine; H | 2015 |
Synthetic, Register-Specific, AAB Heterotrimers to Investigate Single Point Glycine Mutations in Osteogenesis Imperfecta.
Topics: Amino Acid Substitution; Collagen Type I; Glycine; Molecular Dynamics Simulation; Oligopeptides; Ost | 2016 |
Decreased fracture rate, pharmacogenetics and BMD response in 79 Swedish children with osteogenesis imperfecta types I, III and IV treated with Pamidronate.
Topics: Body Height; Bone Density; Child; Child, Preschool; Collagen Type I; Diphosphonates; DNA Mutational | 2016 |
Eight mutations including 5 novel ones in the COL1A1 gene in Czech patients with osteogenesis imperfecta.
Topics: Adolescent; Adult; Amino Acid Substitution; Child; Collagen Type I; Collagen Type I, alpha 1 Chain; | 2016 |
Single molecule effects of osteogenesis imperfecta mutations in tropocollagen protein domains.
Topics: Amino Acid Substitution; Analysis of Variance; Biomechanical Phenomena; Computer Simulation; Elastic | 2009 |
Osteogenesis imperfecta type III with intracranial hemorrhage and brachydactyly associated with mutations in exon 49 of COL1A2.
Topics: Adolescent; Amino Acid Sequence; Child; Cohort Studies; Collagen Type I; DNA Mutational Analysis; Ex | 2009 |
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 |
Molecular and mesoscale mechanisms of osteogenesis imperfecta disease in collagen fibrils.
Topics: Computer Simulation; Elastic Modulus; Elasticity; Fibrillar Collagens; Glycine; Humans; Models, Biol | 2009 |
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 | 2011 |
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 |
Osteogenesis imperfecta model peptides: incorporation of residues replacing Gly within a triple helix achieved by renucleation and local flexibility.
Topics: Amino Acid Sequence; Amino Acid Substitution; Collagen Type I; Diffusion; Glycine; Magnetic Resonanc | 2011 |
Osteogenesis imperfecta missense mutations in collagen: structural consequences of a glycine to alanine replacement at a highly charged site.
Topics: Alanine; Amino Acid Substitution; Calorimetry, Differential Scanning; Circular Dichroism; Collagen T | 2011 |
Identification of a missense mutation of c.3064G>A, Gly1022Ser in exon 43 of COL1A1 gene in a girl with osteogenesis imperfecta type III.
Topics: Child; Collagen Type I; Collagen Type I, alpha 1 Chain; Exons; Female; Genotype; Glycine; Humans; Mu | 2012 |
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 Tempe | 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 |
Severity of osteogenesis imperfecta and structure of a collagen-like peptide modeling a lethal mutation site.
Topics: Amino Acid Sequence; Amino Acid Substitution; Collagen; Collagen Type I; Computer Simulation; Genes, | 2004 |
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 Stabilit | 2004 |
Biochemical screening of type I collagen in osteogenesis imperfecta: detection of glycine substitutions in the amino end of the alpha chains requires supplementation by molecular analysis.
Topics: Adolescent; Adult; Amino Acid Substitution; Cells, Cultured; Child; Child, Preschool; Collagen Type | 2006 |
Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations.
Topics: Amino Acid Substitution; Circular Dichroism; Collagen Type I; Collagen Type I, alpha 1 Chain; Glycin | 2008 |
Osteogenesis imperfecta collagen-like peptides: self-assembly and mineralization on surfaces.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Calcification, Physiologic; Calcium Phosphate | 2008 |
[Osteogenesis imperfecta with ketone hyperglycinemia, hyperserinemia and hyperornithinemia].
Topics: Child; Female; Glycine; Humans; Ornithine; Osteogenesis Imperfecta; Serine | 1980 |
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 Bromi | 1995 |
Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910-->Ala substitution in the alpha 1 (I) chain.
Topics: Alanine; Collagen; Cyanogen Bromide; Deoxyribonuclease HpaII; Deoxyribonucleases, Type II Site-Speci | 1993 |
Two additional cases of osteogenesis imperfecta with substitutions for glycine in the alpha 2(I) collagen chain. A regional model relating mutation location with phenotype.
Topics: Amino Acid Sequence; Base Sequence; Child, Preschool; Collagen; Cyanogen Bromide; DNA; Female; Glyci | 1993 |
A novel G1006A substitution in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III.
Topics: Alanine; Base Sequence; Collagen; Female; Glycine; Heterozygote; Humans; Male; Molecular Sequence Da | 1995 |
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 |
Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix.
Topics: Base Sequence; Child; Child, Preschool; Collagen; Female; Glycine; Humans; Male; Molecular Sequence | 1994 |
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 Da | 1994 |
A novel glycine to glutamic acid substitution at position 343 in the alpha 2 chain of type I collagen in an individual with lethal osteogenesis imperfecta.
Topics: Amino Acid Sequence; Base Sequence; Collagen; DNA; DNA Primers; Female; Genes, Lethal; Glutamates; G | 1993 |
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 Se | 1994 |
Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by p
Topics: Amino Acid Sequence; Base Sequence; Child, Preschool; DNA Primers; DNA, Complementary; Electrophores | 1994 |
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; Inf | 1994 |
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 |
SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II.
Topics: Base Sequence; DNA Mutational Analysis; DNA, Single-Stranded; Electrophoresis, Polyacrylamide Gel; G | 1993 |
Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta.
Topics: Amino Acid Sequence; Cells, Cultured; Collagen; Cysteine; Fibroblasts; Glycine; Kinetics; Osteogenes | 1994 |
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 | 1994 |
Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion.
Topics: Adult; Base Sequence; Chymotrypsin; Collagen; Drug Stability; Endopeptidases; Glycine; Hot Temperatu | 1993 |
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; F | 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 |
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, | 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 |
Arachnoid cyst and chronic subdural haematoma in a child with osteogenesis imperfecta type III resulting from the substitution of glycine 1006 by alanine in the pro alpha 2(I) chain of type I procollagen.
Topics: Adult; Alanine; Arachnoid Cysts; Female; Genetic Carrier Screening; Glycine; Hematoma, Subdural; Hum | 1996 |
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; Ele | 1996 |
Disrupted growth plates and progressive deformities in osteogenesis imperfecta as a result of the substitution of glycine 585 by valine in the alpha 2 (I) chain of type I collagen.
Topics: Adolescent; Adult; Arm; Bone and Bones; Child, Preschool; Collagen; Female; Glycine; Growth Plate; H | 1996 |
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 |
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; C | 1997 |
Three novel type I collagen mutations in osteogenesis imperfecta type IV probands are associated with discrepancies between electrophoretic migration of osteoblast and fibroblast collagen.
Topics: Adolescent; Amino Acid Sequence; Cells, Cultured; Child; Child, Preschool; Collagen; Cyanogen Bromid | 1998 |
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 |
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; Oste | 1998 |
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; | 1999 |
Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes. Mutations in brief no. 152. Online.
Topics: Amino Acid Substitution; Collagen; Genes, Lethal; Glycine; Humans; Osteogenesis Imperfecta | 1998 |
Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine.
Topics: Amino Acid Substitution; Circular Dichroism; Collagen; Glycine; Humans; Osteogenesis Imperfecta; Pep | 2000 |
Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation.
Topics: Adult; Amino Acid Substitution; Child; Collagen; Female; Glycine; Humans; Male; Osteogenesis Imperfe | 2000 |
Sequence of normal canine COL1A1 cDNA and identification of a heterozygous alpha1(I) collagen Gly208Ala mutation in a severe case of canine osteogenesis imperfecta.
Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; Collagen; Collagen Type I; Collagen Type I, al | 2000 |
G76E substitution in type I collagen is the first nonlethal glutamic acid substitution in the alpha1(I) chain and alters folding of the N-terminal end of the helix.
Topics: Adolescent; Amino Acid Substitution; Bone and Bones; Cells, Cultured; Collagen; DNA Primers; Electro | 2001 |
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 Ty | 2001 |
Disturbance in the regulation of the type of collagen synthesized in a form of osteogenesis imperfecta.
Topics: Cells, Cultured; Collagen; Fibroblasts; Fluorescent Antibody Technique; Glycine; Humans; Osteogenesi | 1975 |
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; El | 1992 |
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; Fibrobl | 1992 |
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; G | 1992 |
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 |
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, | 1992 |
A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta.
Topics: Alleles; Base Sequence; Collagen; Collagen Type I, alpha 1 Chain; Female; Genes, Dominant; Genetic C | 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; Kineti | 1992 |
The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen.
Topics: Adult; Amino Acid Sequence; Female; Fetus; Glycine; Humans; Infant, Newborn; Male; Molecular Sequenc | 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 |
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; | 1991 |
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, | 1992 |
Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix.
Topics: Alleles; Base Sequence; DNA; Electrophoresis, Polyacrylamide Gel; Female; Genes, Lethal; Glycine; Ho | 1991 |
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, New | 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 Te | 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; Gl | 1991 |
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, Let | 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; Huma | 1991 |
Characterization of a type I collagen alpha 2(I) glycine-586 to valine substitution in osteogenesis imperfecta type IV. Detection of the mutation and prenatal diagnosis by a chemical cleavage method.
Topics: Amino Acid Sequence; Base Sequence; Cells, Cultured; Child; Chorionic Villi; Collagen; Female; Glyci | 1991 |
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 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; G | 1990 |
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 De | 1990 |
Human genetics. Bone disease cracks genetics.
Topics: Codon; Collagen; Exons; Glycine; Humans; Mutation; Osteogenesis Imperfecta | 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 |
Correlation of clinical and molecular biological abnormalities in osteogenesis imperfecta.
Topics: Alanine; Arginine; Genotype; Glycine; Humans; Infant; Mutation; Osteogenesis Imperfecta; Phenotype; | 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; O | 1989 |
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; Cyste | 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; Midd | 1988 |
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; Molec | 1989 |
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; | 1989 |
Dentine is biochemically abnormal in osteogenesis imperfecta.
Topics: Amino Acids; Dentin; Glycine; Humans; Hydroxyproline; Lysine; Osteogenesis Imperfecta | 1986 |
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, Polyacry | 1987 |
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 | 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; Hum | 1988 |
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; Infa | 1988 |
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 Temp | 1987 |
The amino-acid composition of human hard tissue collagens in osteogenesis imperfecta and dentinogenesis imperfecta.
Topics: Alanine; Amino Acids; Bone and Bones; Child; Collagen; Dentin; Dentinogenesis Imperfecta; Glycine; H | 1973 |