Interaction of prolyl 4-hydroxylase with synthetic peptide substrates. A conformational model for collagen proline hydroxylation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference50 articles.
1. Protein hydroxylation: prolyl 4‐hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit
2. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
3. Conformational implications of enzymatic proline hydroxylation in collagen.
4. Photoaffinity labeling of peptide binding sites of prolyl 4-hydroxylase with N-(4-azido-2-nitrophenyl)glycyl-(Pro-Pro-Gly)5
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1. Prolyl 4-Hydroxylase: Substrate Isosteres in Which an (E)- or (Z)-Alkene Replaces the Prolyl Peptide Bond;Biochemistry;2016-12-21
2. Investigating the Role of (2S,4R)-4-Hydroxyproline in Elastin Model Peptides;Biomacromolecules;2013-11-04
3. Design and Production of a Chimeric Resilin-, Elastin-, and Collagen-Like Engineered Polypeptide;Biomacromolecules;2011-07-08
4. Prolyl 4-hydroxylase;Critical Reviews in Biochemistry and Molecular Biology;2010-03-04
5. Conformational Preferences of Substrates for Human Prolyl 4-Hydroxylase;Biochemistry;2008-08-15
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