Trimerization of the Amino Propeptide of Type IIA Procollagen Using a 14-Amino Acid Sequence Derived from the Coiled-Coil Neck Domain of Surfactant Protein D-Reference-Cited by-同舟云学术

Trimerization of the Amino Propeptide of Type IIA Procollagen Using a 14-Amino Acid Sequence Derived from the Coiled-Coil Neck Domain of Surfactant Protein D

Published:2002-10 Issue:43 Volume:277 Page:41274-41281
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

McAlinden Audrey,Crouch Erika C.,Bann James G.,Zhang Pengnian,Sandell Linda J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Differential expression of a cysteine-rich domain in the amino-terminal propeptide of type II (cartilage) procollagen by alternative splicing of mRNA.

2. Organization of the exons coding for pro α1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes

3. Endoplasmic Reticulum-mediated Quality Control of Type I Collagen Production by Cells from Osteogenesis Imperfecta Patients with Mutations in the proα1(I) Chain Carboxyl-terminal Propeptide which Impair Subunit Assembly

4. Folding of carboxyl domain and assembly of procollagen I.

5. Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta.

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