Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern.-Reference-Cited by-同舟云学术

Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern.

Published:1992-04 Issue:11 Volume:267 Page:7751-7757
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chessler S.D.,Byers P.H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference27 articles.

1. Regulation of Protein Export From the Endoplasmic Reticulum

2. Control of Protein Exit from the Endoplasmic Reticulum

3. Protein degradation in the endoplasmic reticulum

4. Protein Folding: Deciphering the Second Half of the Genetic Code;Byers,1990

5. Osteogenesis imperfecta: translation of mutation to phenotype.

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