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The Crystal Structure of an Algal Prolyl 4-Hydroxylase Complexed with a Proline-rich Peptide Reveals a Novel Buried Tripeptide Binding MotifThe active site of an algal prolyl 4-hydroxylase has a large structural plasticityThe peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residuesIdentification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzymeReorganizing the protein space at the Universal Protein Resource (UniProt)The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase.Chlamydomonas reinhardtii has multiple prolyl 4-hydroxylases, one of which is essential for proper cell wall assembly.
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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Reija Hieta
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0000-0001-5724-6253