ReviewArchives of biochemistry and biophysics2012
Allosteric regulation of phenylalanine hydroxylase.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 66 citations in OpenAlex.
- DNAJC12 Stabilizes Phenylalanine Hydroxylase and Facilitates Its Substrate-Dependent Activation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Enhancement of therapeutic transgene insertion for treatment of murine phenylketonuria.Molecular therapy. Nucleic acids · 2026Article
- From structural insight to molecule: Integrative molecular simulations identify candidate pyruvate kinase activators.PloS one · 2026Article
- Phenylalanine Regulates Milk Protein Synthesis via LAT1-mTOR Signaling Pathways in Bovine Mammary Epithelial Cells.International journal of molecular sciences · 2024Article
- Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum.Archives of biochemistry and biophysics · 2022Article
- Manipulation of a cation-π sandwich reveals conformational flexibility in phenylalanine hydroxylase.Biochimie · 2021Article
- Animal Model Contributions to Congenital Metabolic Disease.Advances in experimental medicine and biology · 2020Review
- Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability.Scientific reports · 2019Article
- Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.The Journal of biological chemistry · 2019Article
- Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.The Journal of biological chemistry · 2019Article
- Phosphorylation of Phenylalanine Hydroxylase Increases the Rate Constant for Formation of the Activated Conformation of the Enzyme.Biochemistry · 2018Article
- New protein structures provide an updated understanding of phenylketonuria.Molecular genetics and metabolism · 2017Review
- X-ray Scattering Studies of Protein Structural Dynamics.Chemical reviews · 2017Review
- The regulatory domain of human tryptophan hydroxylase 1 forms a stable dimer.Biochemical and biophysical research communications · 2016Article
- Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.Journal of the American Chemical Society · 2016Article
- Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Scientific reports · 2016Article
- Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase.The Journal of biological chemistry · 2016Article
- First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- First Case Report of EX3del4765 Mutation in PAH Gene in Asian Population.Iranian Red Crescent medical journal · 2016Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin. Phosphorylation of Ser16 lowers the concentration of phenylalanine for activation. This review discusses the present understanding of the molecular details of the allosteric regulation of the enzyme.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.