Associated Papers
Frequency enrichment of coding variants in a French-Canadian founder population and its implication for inflammatory bowel diseases.
Bhérer C et al.
Medrxiv : the Preprint Server for Health Sciences, 2025
Protein domains provide a new layer of information for classifying human variations in rare diseases.
Corcuff M et al.
Frontiers in Bioinformatics, 2023
Dictyostelium discoideum Ax2 as an Assay System for Screening of Pharmacological Chaperones for Phenylketonuria Mutations.
Kim YM et al.
Journal of Microbiology and Biotechnology, 2015
Protein stability and in vivo concentration of missense mutations in phenylalanine hydroxylase.
Shi Z et al.
Proteins, 2012
Homomeric and heteromeric interactions between wild-type and mutant phenylalanine hydroxylase subunits: evaluation of two-hybrid approaches for functional analysis of mutations causing hyperphenylalaninemia.
Waters PJ et al.
Molecular Genetics and Metabolism, 2001
The role of chaperone-assisted folding and quality control in inborn errors of metabolism: protein folding disorders.
Gregersen N et al.
Journal of Inherited Metabolic Disease, 2001
Structural interpretation of mutations in phenylalanine hydroxylase protein aids in identifying genotype-phenotype correlations in phenylketonuria.
Jennings IG et al.
European Journal of Human Genetics : Ejhg, 2000
Defective folding and rapid degradation of mutant proteins is a common disease mechanism in genetic disorders.
Gregersen N et al.
Journal of Inherited Metabolic Disease, 2000
Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype.
Waters PJ et al.
Molecular Genetics and Metabolism, 2000
Missense mutations in the phenylalanine hydroxylase gene (PAH) can cause accelerated proteolytic turnover of PAH enzyme: a mechanism underlying phenylketonuria.
Waters PJ et al.
Journal of Inherited Metabolic Disease, 1999
Mutation at the phenylalanine hydroxylase gene (PAH) and its use to document population genetic variation: the Quebec experience.
Carter KC et al.
European Journal of Human Genetics : Ejhg, 1998
Alterations in protein aggregation and degradation due to mild and severe missense mutations (A104D, R157N) in the human phenylalanine hydroxylase gene (PAH).
Waters PJ et al.
Human Mutation, 1998
Human phenylalanine hydroxylase mutations and hyperphenylalaninemia phenotypes: a metanalysis of genotype-phenotype correlations.
Kayaalp E et al.
American Journal of Human Genetics, 1997
Identical SRY mutations with different phenotypic effects.
Mittwoch U
American Journal of Human Genetics, 1993