Intracellular trafficking and degradation of unassociated proα2 chains of collagen type I
✍ Scribed by Marilyn G Gotkin; Catherine R Ripley; Shireen R Lamande; John F Bateman; Robert S Bienkowski
- Book ID
- 116980943
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 854 KB
- Volume
- 296
- Category
- Article
- ISSN
- 0014-4827
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📜 SIMILAR VOLUMES
Procollagen (Type I) contains a noncollagenous COOH-terminal propeptide (C-propeptide) hypothesized to be important in directing chain association and alignment during assembly. We previously expressed human pro-␣2(I) cDNA in rat liver epithelial cells, W8, that produce only pro-␣1(I) trimer collage
Collagen biosynthesis is a complex process that begins with the association of three procollagen chains. A series of conserved intra-and interchain disulfide bonds in the carboxyl-terminal region of the procollagen chains, or C-propeptide, has been hypothesized to play an important role in the nucle