The Role of Disulfide Bonds and α-Helical Coiled-coils in the Biosynthesis of Type XIII Collagen and Other Collagenous Transmembrane Proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*
2. Type XIII Collagen Forms Homotrimers with Three Triple Helical Collagenous Domains and Its Association into Disulfide-bonded Trimers Is Enhanced by Prolyl 4-Hydroxylase
3. A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins
4. Type XIII Collagen and Some Other Transmembrane Collagens Contain Two Separate Coiled-coil Motifs, Which May Function as Independent Oligomerization Domains
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