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August 15, 1992Proceedings of the National Academy of SciencesOpen Access

Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.

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Authors

KVKristiina A. VuoriUniversity of HelsinkiTPTaina PihlajaniemiOulu University of Applied SciencesMMMinna MarttilaKyoto University

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Vuori et al. (1992) studied this question.

synapsesocial.com/papers/6a9908f1aa63da60ef78cba4https://doi.org/10.1073/pnas.89.16.7467
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity.1992 · 147 citations
  2. 2Purification and characterization of a thiol:protein disulfide oxidoreductase from bovine liver.1977 · 81 citations
  3. 3Protein hydroxylation: prolyl 4‐hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit1989 · 320 citations
  4. 4A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase.1987 · 240 citations
  5. 5Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen.1991 · 77 citations