Missense Mutations in the N-Terminal Domain of Human Phenylalanine Hydroxylase Interfere with Binding of Regulatory Phenylalanine

This publication has 32 references indexed in Scilit:

• In Vitro Expression of 34 Naturally Occurring Mutant Variants of Phenylalanine Hydroxylase: Correlation with Metabolic Phenotypes and Susceptibility toward Protein Aggregation
  Molecular Genetics and Metabolism, 2001
• Mutagenesis of the regulatory domain of phenylalanine hydroxylase
  Proceedings of the National Academy of Sciences, 2001
• Essential role of the N‐terminal autoregulatory sequence in the regulation of phenylalanine hydroxylase
  FEBS Letters, 2001
• Structural interpretation of mutations in phenylalanine hydroxylase protein aids in identifying genotype–phenotype correlations in phenylketonuria
  European Journal of Human Genetics, 2000
• Characterization of Phenylketonuria Missense Substitutions, Distant from the Phenylalanine Hydroxylase Active Site, Illustrates a Paradigm for Mechanism and Potential Modulation of Phenotype
  Molecular Genetics and Metabolism, 2000
• Urea-induced Denaturation of Human Phenylalanine Hydroxylase
  Published by Elsevier ,1999
• Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme
  Biochemical Journal, 1995
• The Phenylalanine Hydroxylating System
  Published by Wiley ,1993
• A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila.
  Journal of Biological Chemistry, 1992
• Relationship between the substrate activation site and catalytic site of phenylalanine hydroxylase.
  Journal of Biological Chemistry, 1980