A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase.
Open Access
- 1 December 1992
- journal article
- case report
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (35) , 25529-25534
- https://doi.org/10.1016/s0021-9258(19)74072-1
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Osteogenesis imperfecta: translation of mutation to phenotype.Journal of Medical Genetics, 1991
- Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen predicts an elongated Pro alpha 1(I) chain and results in osteogenesis imperfecta type I.Journal of Clinical Investigation, 1990
- Influence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptidesBiopolymers, 1986
- Structural study of a mutant type I collagen from a patient with lethal osteogenesis imperfecta containing an intramolecular disulfide bond in the triple‐helical domainFEBS Letters, 1986
- Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type IINature, 1985
- Mica sandwich technique for preparing macromolecules for rotary shadowingJournal of Ultrastructure Research, 1985
- Conformational stability of type I collagen triple helix: Evidence for temporary and local relaxation of the protein conformation using a proteolytic probeArchives of Biochemistry and Biophysics, 1983
- Proteolytic enzymes as probes for the triple-helical conformation of procollagenAnalytical Biochemistry, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acidArchives of Biochemistry and Biophysics, 1961