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Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans
TLDR
The data on genotype–phenotype relationships indicate that the two collagen chains play very different roles in matrix integrity and that phenotype depends on intracellular and extracellular events. Expand
New perspectives on osteogenesis imperfecta
TLDR
Clinical management of osteogenesis imperfecta is multidisciplinary, encompassing substantial progress in physical rehabilitation and surgical procedures, management of hearing, dental and pulmonary abnormalities, as well as drugs, such as bisphosphonates and recombinant human growth hormone. Expand
Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta
TLDR
The first five cases of a new recessive bone disorder resulting from null LEPRE1 alleles are presented; its phenotype overlaps with lethal/severe osteogenesis imperfecta but has distinctive features and a mutant allele from West Africa occurs in four of five cases. Expand
Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta.
TLDR
Three of 10 children with lethal or severe osteogenesis imperfecta were found to have a recessive condition resulting in CRTAP deficiency, suggesting that prolyl 3-hydroxylation of type I collagen is important for bone formation. Expand
Candidate Cell and Matrix Interaction Domains on the Collagen Fibril, the Predominant Protein of Vertebrates*
TLDR
The fibril domain model provides potential insights into the genotype-phenotype relationship for several classes of human connective tissue diseases, mechanisms of integrin clustering by fibrils, the polarity of fibrill assembly, heterotypic fibrIL function, and connectedive tissue pathology in diabetes and aging. Expand
Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding.
TLDR
The proband's collagen had normal collagen folding and normal prolyl 3-hydroxylation, suggesting that CyPB is not the exclusive peptidyl-prolyl cis-trans isomerase that catalyzes the rate-limiting step in collagen folding, as is currently thought. Expand
Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta
TLDR
It is shown that the long-sought cause of the recessive form of OI, first postulated in the Sillence classification, lies in defects in the genes encoding cartilage-associated protein (CRTAP) or prolyl 3-hydroxylase 1 (P3H1/LEPRE1). Expand
Components of the Collagen Prolyl 3-Hydroxylation Complex are Crucial for Normal Bone Development
TLDR
The critical importance of the components of the prolyl 3-hydroxylation complex for normal bone development has been revealed by a Crtap knock-out mouse and by infants and children with null mutations of CRTAP and LEPRE1, the gene that encodes P3H1. Expand
Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross‐linking and reduced collagen deposition in extracellular matrix
TLDR
Mass spectrometry reveals absence of hydroxylation of the collagen telopeptide lysine involved in cross‐linking, suggesting that FKBP65 is required for lysyl hydroxymase activity or access to type I collagen telopesine lysines, perhaps through its function as a peptidylprolyl isomerase. Expand
Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex.
TLDR
Mutual stabilization of P3H1 and CRTAP in the ER collagen modification complex is an underlying mechanism for the overlapping phenotype of types VII and VIII OI. Expand
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