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A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeuticsAn additional substrate binding site in a bacterial phenylalanine hydroxylaseStructural and thermodynamic insight into phenylalanine hydroxylase from the human pathogenLegionella pneumophilaThe Solution Structure of the Regulatory Domain of Tyrosine HydroxylaseStructural insights into the regulation of aromatic amino acid hydroxylationA synopsis on the role of tyrosine hydroxylase in Parkinson's diseaseX-ray Scattering Studies of Protein Structural Dynamics.Protein homeostasis disorders of key enzymes of amino acids metabolism: mutation-induced protein kinetic destabilization and new therapeutic strategies.The Concise Guide to PHARMACOLOGY 2013/14: enzymes.A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis.Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulationPhenylalanine hydroxylase misfolding and pharmacological chaperones.Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase.Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active siteThe Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers.First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramerIdentification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase.Impact of quaternary structure dynamics on allosteric drug discovery.First Case Report of EX3del4765 Mutation in PAH Gene in Asian Population.Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.Phenylalanine hydroxylase: function, structure, and regulation.Understanding allosteric and cooperative interactions in enzymes.Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Computational study of missense mutations in phenylalanine hydroxylase.Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.Mutagenesis of a specificity-determining residue in tyrosine hydroxylase establishes that the enzyme is a robust phenylalanine hydroxylase but a fragile tyrosine hydroxylaseRegulation of phenylalanine hydroxylase: conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry.The regulatory domain of human tryptophan hydroxylase 1 forms a stable dimerTowards the identification of the allosteric Phe-binding site in phenylalanine hydroxylase.Dictyostelium phenylalanine hydroxylase is activated by its substrate phenylalanine.Performance of piglets in response to the standardized ileal digestible phenylalanine and tyrosine supply in low-protein diets
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P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Allosteric regulation of phenylalanine hydroxylase.
@en
Allosteric regulation of phenylalanine hydroxylase.
@nl
type
label
Allosteric regulation of phenylalanine hydroxylase.
@en
Allosteric regulation of phenylalanine hydroxylase.
@nl
prefLabel
Allosteric regulation of phenylalanine hydroxylase.
@en
Allosteric regulation of phenylalanine hydroxylase.
@nl
P2860
P1476
Allosteric regulation of phenylalanine hydroxylase.
@en
P2093
Paul F Fitzpatrick
P2860
P304
P356
10.1016/J.ABB.2011.09.012
P407
P577
2011-10-07T00:00:00Z