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

Volumn 69, Issue 2, 2000, Pages 101-110

  Waters, Paula J ^a,b   Parniak, Michael A ^b,c   Akerman, Beverly R ^a   Scriver, Charles R ^a,b  

^a MONTREAL CHILDREN S HOSPITAL   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c MCGILL UNIVERSITY   (Canada)

Author keywords

Aggregation; Crystal structure; Hyperphenylalaninemia; In vitro expression; Missense mutations; Phenotypic variability; Phenylalanine hydroxylase; Protein degradation

Indexed keywords

M PROTEIN; PHENYLALANINE 4 MONOOXYGENASE;

ALLELE; AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CELL AGGREGATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; MISSENSE MUTATION; OLIGOMERIZATION; PHENOTYPE; PHENYLKETONURIA; PREDICTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION;

EID: 0034110962     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1006/mgme.2000.2965     Document Type: Article

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