Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

New protein structures provide an updated understanding of phenylketonuria.

Molecular genetics and metabolism - 1 Aug 2017

Jaffe Eileen K

Abstract excerpt

Phenylketonuria (PKU) and less severe hyperphenylalaninemia (HPA) constitute the most common inborn error of amino acid metabolism, and is most often caused by defects in phenylalanine hydroxylase (PAH) function resulting in accumulation of Phe to neurotoxic levels. Despite the success of dietary intervention in preventing permanent neurological damage, individuals living with PKU clamor for additional...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Regulation
Share to Biopterins
Share to Mutation, Missense

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Phenylalanine

Share to Phenylalanine Hydroxylase

Share to Phenylketonurias

Share to Protein Folding

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 28645531
DOI: 10.1016/j.ymgme.2017.06.005
PMCID: PMC5549558

Genes

PAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

New protein structures provide an updated understanding of phenylketonuria.PMID 28645531Read ↗

Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype.Semantic proximity Read ↗

Natural phenylalanine hydroxylase variants that confer a mild phenotype affect the enzyme's conformational stability and oligomerization equilibrium.Semantic proximity Read ↗

Structural interpretation of mutations in phenylalanine hydroxylase protein aids in identifying genotype-phenotype correlations in phenylketonuria.Semantic proximity Read ↗

Structural Insights into the Mechanisms Underlying Polyaminopathies.Semantic proximity Read ↗

The structural basis of phenylketonuria.Semantic proximity Read ↗

Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases.Semantic proximity Read ↗

DNAJC12 stabilizes activated phenylalanine hydroxylase and reduces the concentration of L-Phe needed for activationSemantic proximity Read ↗

The structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterinSemantic proximity Read ↗

Hyperphenylalaninemia in the Czech Republic: genotype-phenotype correlations and in silico analysis of novel missense mutations.Semantic proximity Read ↗

Pahenu1 is a mouse model for tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency and promotes analysis of the pharmacological chaperone mechanism in vivo.Semantic proximity Read ↗

Structural studies on phenylalanine hydroxylase and implications toward understanding and treating phenylketonuria.Semantic proximity Read ↗

Variant-dependent pharmacological rescue of phenylalanine hydroxylase supports a precision therapeutic strategy for phenylketonuria.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.