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March 1, 1989The FASEB Journal

Protein hydroxylation: prolyl 4‐hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit

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Authors

KKKari I. KivirikkoRutgers, The State University of New JerseyRMRaili MyllyläAcademy of Medical SciencesTPTaina PihlajaniemiOulu University of Applied Sciences

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Cite This Study

Kivirikko et al. (1989) studied this question.

synapsesocial.com/papers/6a6f5fe5febe604dd7084f02https://doi.org/10.1096/fasebj.3.5.2537773
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Also Consider

Synapse has enriched 3 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase.1984 · 244 citations
  2. 2Two distinct classes of carbohydrate-recognition domains in animal lectins.1988 · 1,263 citations
  3. 3Biosynthesis of prolyl hydroxylase: evidence for two separate dolichol-mediated pathways of glycosylation1985 · 26 citations