Associated Papers
Integrated clinical and omics approach to rare diseases: novel genes and oligogenic inheritance in holoprosencephaly.
Kim A et al.
Brain : a Journal of Neurology, 2019
Relationship between genotype, phenylalanine hydroxylase expression and in vitro activity and metabolic phenotype in phenylketonuria.
Himmelreich N et al.
Molecular Genetics and Metabolism, 2018
Tetrahydrobiopterin, its mode of action on phenylalanine hydroxylase, and importance of genotypes for pharmacological therapy of phenylketonuria.
Heintz C et al.
Human Mutation, 2013
Protein stability and in vivo concentration of missense mutations in phenylalanine hydroxylase.
Shi Z et al.
Proteins, 2012
Molecular genetics and impact of residual in vitro phenylalanine hydroxylase activity on tetrahydrobiopterin responsiveness in Turkish PKU population.
Dobrowolski SF et al.
Molecular Genetics and Metabolism, 2011
Biochemical characterization of mutant phenylalanine hydroxylase enzymes and correlation with clinical presentation in hyperphenylalaninaemic patients.
Dobrowolski SF et al.
Journal of Inherited Metabolic Disease, 2009
PAHdb 2003: what a locus-specific knowledgebase can do.
Scriver CR et al.
Human Mutation, 2003
How PAH gene mutations cause hyper-phenylalaninemia and why mechanism matters: insights from in vitro expression.
Waters PJ
Human Mutation, 2003
Missense mutations in the N-terminal domain of human phenylalanine hydroxylase interfere with binding of regulatory phenylalanine.
Gjetting T et al.
American Journal of Human Genetics, 2001
A structural hypothesis for BH4 responsiveness in patients with mild forms of hyperphenylalaninaemia and phenylketonuria.
Erlandsen H 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
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
Phenylalanine and tyrosine metabolism in phenylketonuria heterozygotes: influence of different phenylalanine hydroxylase mutations.
Spada M et al.
Journal of Inherited Metabolic Disease, 1998
PAH Mutation Analysis Consortium Database: 1997. Prototype for relational locus-specific mutation databases.
Nowacki PM et al.
Nucleic Acids Research, 1998
In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function.
Waters PJ et al.
Human Mutation, 1998
Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene.
Lüdecke B et al.
Human Molecular Genetics, 1996
Phenylketonuria genotypes correlated to metabolic phenotype groups in Norway.
Eiken HG et al.
European Journal of Pediatrics, 1996
PKU mutation G46S is associated with increased aggregation and degradation of the phenylalanine hydroxylase enzyme.
Eiken HG et al.
Human Mutation, 1996
Relative frequency, heterogeneity and geographic clustering of PKU mutations in Norway.
Eiken HG et al.
European Journal of Human Genetics : Ejhg, 1996
PKU mutation (D143G) associated with an apparent high residual enzyme activity: expression of a kinetic variant form of phenylalanine hydroxylase in three different systems.
Knappskog PM et al.
Human Mutation, 1996
[Mutation analysis of the phenylalanine hydroxylase gene of phenylketonuria patients of Kemerovskaya Oblast' and Saha Republic].
Baturina OA et al.
Tsitologiia I Genetika, 0
Assessment of the Phenylketonuria (PKU)-Associated Mutation p.R155H Biochemical Manifestations by Mass Spectrometry-Based Blood Metabolite Profiling.
Baturina OA et al.
Acta Naturae, 0