Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium-Reference-Cited by-同舟云学术

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Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium

Published:2019-06 Issue:26 Volume:294 Page:10131-10145
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Arturo Emilia C.^ORCID,Gupta Kushol,Hansen Michael R.,Borne Elias,Jaffe Eileen K.^ORCID

Funder

HHS | NIH | National Institute of Neurological Disorders and Stroke (NINDS)

National PKU Alliance (NPKUA)

NIH/NCI Cancer Center

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference71 articles.

1. Genetics of phenylketonuria: then and now;Blau;Hum. Mutat,2016

2. The ACT domain family;Chipman;Curr. Opin. Struct. Biol,2001

3. The ACT domain: a small molecule binding domain and its role as a common regulatory element;Grant;J. Biol. Chem,2006

4. Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism;Lang;Curr. Opin. Struct. Biol,2014

5. New protein structures provide an updated understanding of phenylketonuria;Jaffe;Mol. Genet. Metab,2017

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1. Unveiling the genetic tapestry: Rare disease genomics of spinal muscular atrophy and phenylketonuria proteins;International Journal of Biological Macromolecules;2024-06

2. Biochemical and biophysical approaches to characterization of the aromatic amino acid hydroxylases;Methods in Enzymology;2024

3. Unveiling the Genetic Tapestry: Rare Disease Genomics of Spinal Muscular Atrophy and Phenylketonuria Proteins;2023-11-28

4. Structural characterization of human tryptophan hydroxylase 2 reveals that L-Phe is superior to L-Trp as the regulatory domain ligand;Structure;2023-06

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