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July 1, 1996Biochemical JournalOpen Access

Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation

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Authors

NBNeil J. BulleidUniversity of GlasgowRWRichard WilsonUniversity of TasmaniaJLJanice F. LeesUniversity of Manchester

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Cite This Study

Bulleid et al. (1996) studied this question.

synapsesocial.com/papers/6a9bd83dafec4d880bfb4c25https://doi.org/10.1042/bj3170195
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Also Consider

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  1. 1The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen.1994 · 69 citations
  2. 2Folding Mechanism of the Triple Helix in Type‐III Collagen and Type‐III pN–Collagen1980 · 275 citations
  3. 3Structure of a full-length cDNA clone for the preproα2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation1988 · 129 citations
  4. 4Time of occurrence of disulfide linking between procollagen chains.1976 · 31 citations
  5. 5Defective 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.1992 · 67 citations