PKU mutation p.G46S prevents the stereospecific binding ofl-phenylalanine to the dimer of human phenylalanine hydroxylase regulatory domain

Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase

(2016) Shengnan Zhang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering

(2016) Steve P. Meisburger et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer

(2016) Emilia C. Arturo et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain

(2016) Dipali Patel et al.   Scientific Reports

Structural insights into the regulation of aromatic amino acid hydroxylation

(2015) Paul F Fitzpatrick   CURRENT OPINION IN STRUCTURAL BIOLOGY

Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase

(2014) Shengnan Zhang et al.   BIOCHEMISTRY

Activation of Phenylalanine Hydroxylase by Phenylalanine Does Not Require Binding in the Active Site

(2014) Kenneth M. Roberts et al.   BIOCHEMISTRY

Superstoichiometric binding of L-Phe to phenylalanine hydroxylase from Caenorhabditis elegans: evolutionary implications

(2010) Marte I. Flydal et al.   AMINO ACIDS

Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation

(2010) João Leandro et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE