In general, osteogenesis imperfecta is caused by heterozygous mutations in either of the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively). Usually, these mutations are unique to the affected individual or individuals within a family. In this study, si
Changes in Thermal Stability and Microunfolding Pattern of Collagen Helix Resulting from the Loss of α2(I) Chain in Osteogenesis Imperfecta Murine
✍ Scribed by Natalia V. Kuznetsova; Daniel J. McBride Jr; Sergey Leikin
- Book ID
- 117143420
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 849 KB
- Volume
- 331
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Osteogenesis imperfecta (OI) is a congenital disease of connective tissue, most often caused by single amino acid substitutions of glycine residues within the triple helical region of collagen I. Collagen I consists of two alpha 1 chains and one alpha 2 chain. Thus, a substitution in the alpha 1(I)
## Clinical Data on Patients KO was 35 years of age at the time her cell strain was sent to us. She was born to healthy unrelated parents and has two healthy siblings, both of whom have unaffected children, and no other individuals with 0 1 were identified in the family. She had many fractures at
Triple helix formation is a prerequisite for the passage of type I procollagen from the endoplasmic reticulum and secretion from the cell to form extracellular fibrils that will support mineral deposition in bone. Analysis of cDNA from 11 unrelated individuals with osteogenesis imperfecta (OI) revea