| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Anton V Persikov, Rian J Pillitteri, Priyal Amin, Ulrike Schwarze, Peter H Byers, Barbara Brodsk. Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disorders. Human mutation. vol 24. issue 4. 2005-03-31. PMID:15365990. |
the predicted rates of substitutions by different amino acids for glycine in the alpha1(i), alpha2(i), alpha1(iii), alpha5(iv), and alpha1(vii) chains (encoded by col1a1, col1a2, col3a1, col4a5, and col7a1, respectively) were compared with missense mutations in those chains that have been observed to cause disease. |
2005-03-31 |
2023-08-12 |
Not clear |
| L M Ward, L Lalic, P J Roughley, F H Glorieu. Thirty-three novel COL1A1 and COL1A2 mutations in patients with osteogenesis imperfecta types I-IV. Human mutation. vol 17. issue 5. 2001-08-30. PMID:11317364. |
two rare triple helical gly-->glu substitutions in col1a2 are also described. |
2001-08-30 |
2023-08-12 |
Not clear |
| L M Ward, L Lalic, P J Roughley, F H Glorieu. Thirty-three novel COL1A1 and COL1A2 mutations in patients with osteogenesis imperfecta types I-IV. Human mutation. vol 17. issue 5. 2001-08-30. PMID:11317364. |
most mutations resulted in substitutions for glycine: one of these, a doublet gg>cc transversion, created a unique gly-->pro missense mutation in the triple helical domain of col1a2. |
2001-08-30 |
2023-08-12 |
Not clear |
| L Nuytinck, T Tükel, H Kayserili, M Y Apak, A De Paep. Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation. Journal of medical genetics. vol 37. issue 5. 2000-07-17. PMID:10807697. |
molecular analysis showed a g>t transversion in the col1a2 gene, resulting in the substitution of glycine by tryptophan at position 277 of the alpha2(i) collagen chain. |
2000-07-17 |
2023-08-12 |
Not clear |
| A De Paepe, L Nuytinck, M Raes, J P Fryn. Homozygosity by descent for a COL1A2 mutation in two sibs with severe osteogenesis imperfecta and mild clinical expression in the heterozygotes. Human genetics. vol 99. issue 4. 1997-05-12. PMID:9099837. |
we report two sibs with severe, progressively deforming osteogenesis imperfecta (oi) and homozygosity by descent for a glycine 751 to serine substitution in the alpha2(i) collagen chain due to a g to a transition in the col1a2 gene. |
1997-05-12 |
2023-08-12 |
Not clear |
| M Gomez-Lira, A Sangalli, P F Pignatti, M C Digilio, A Giannotti, E Carnevale, M Motte. 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. Journal of medical genetics. vol 31. issue 12. 1995-04-20. PMID:7891382. |
reverse transcription-polymerase chain reaction dna amplification, followed by cloning and sequencing, showed heterozygosity for a g to t transversion in the first nucleotide of exon 37 of the col1a2 gene, which led to a cysteine for glycine substitution at position 640 of the triple helical domain. |
1995-04-20 |
2023-08-12 |
Not clear |
| L Cohen-Solal, L Zylberberg, A Sangalli, M Gomez Lira, M Motte. 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. The Journal of biological chemistry. vol 269. issue 20. 1994-06-16. PMID:8182080. |
the mutation was identified as a g to a transition in the col1a2 gene, which converts glycine 700 to aspartic acid in the alpha 2i chain. |
1994-06-16 |
2023-08-12 |
Not clear |
| A M Romanic, L D Spotila, E Adachi, J Engel, Y Hojima, D J Procko. Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype. The Journal of biological chemistry. vol 269. issue 15. 1994-05-19. PMID:8157695. |
procollagen i was isolated from cultured skin fibroblasts from a proband who was homozygous for a mutation in the col1a2 gene that substituted a serine codon for a glycine codon at position 661 of the alpha 2(i) chain. |
1994-05-19 |
2023-08-12 |
Not clear |
| M J Edwards, R J Wenstrup, P H Byers, D H Coh. 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. Human mutation. vol 1. issue 1. 1993-05-28. PMID:1301191. |
dna sequence analysis of col1a2 cdnas demonstrated that the cysteine-containing chain resulted from a point mutation (g to t) in the first position of the codon for the glycine at residue 472 of the triple helical domain. |
1993-05-28 |
2023-08-11 |
Not clear |
| R J Wenstrup, L W Lever, C L Phillips, L D Quarle. Mutations in the COL1A2 gene of type I collagen that result in nonlethal forms of osteogenesis imperfecta. American journal of medical genetics. vol 45. issue 2. 1993-04-22. PMID:8456807. |
the relation between position of substitution of glycine by cysteine in the col1a2 gene does not follow the pattern developed in the col1a1 gene. |
1993-04-22 |
2023-08-12 |
mouse |
| B Knebelmann, G Deschenes, F Gros, M C Hors, J P Grünfeld, J Zhou, K Tryggvason, M C Gubler, C Antigna. Substitution of arginine for glycine 325 in the collagen alpha 5 (IV) chain associated with X-linked Alport syndrome: characterization of the mutation by direct sequencing of PCR-amplified lymphoblast cDNA fragments. American journal of human genetics. vol 51. issue 1. 1992-07-23. PMID:1376965. |
it is interesting that such glycine substitutions inside the col1a1 or col1a2 genes have been associated with many cases of osteogenesis imperfecta. |
1992-07-23 |
2023-08-11 |
Not clear |
| D H Cohn, P H Byer. Cysteine in the triple helical domain of the pro alpha 2(I) chain of type-I collagen in nonlethal forms of osteogenesis imperfecta. Human genetics. vol 87. issue 2. 1991-08-13. PMID:2066103. |
these data confirm that individuals with nonlethal oi may commonly harbor defects in the col1a2 gene, and suggest that many of the defects are substitutions for glycine residues in the alpha 2(i) triple helical domain. |
1991-08-13 |
2023-08-11 |
Not clear |
| R J Wenstrup, A W Shrago-Howe, L W Lever, C L Phillips, P H Byers, D H Coh. 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. The Journal of biological chemistry. vol 266. issue 4. 1991-03-07. PMID:1990009. |
a child with a moderately severe form of osteogenesis imperfecta was heterozygous for a g to t transition that resulted in a substitution of cysteine for glycine at position 259 in the col1a2 gene. |
1991-03-07 |
2023-08-11 |
Not clear |
| R J Wenstrup, A W Shrago-Howe, L W Lever, C L Phillips, P H Byers, D H Coh. 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. The Journal of biological chemistry. vol 266. issue 4. 1991-03-07. PMID:1990009. |
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. |
1991-03-07 |
2023-08-11 |
Not clear |
| R J Wenstrup, D H Cohn, T Cohen, P H Byer. 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. The Journal of biological chemistry. vol 263. issue 16. 1988-06-29. PMID:2897363. |
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. |
1988-06-29 |
2023-08-11 |
Not clear |