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

Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene.

Human molecular genetics - 1 Jul 1995

Knappskog P M, Flatmark T, Mallet J, Lüdecke B, Bartholomé K

Abstract excerpt

Tyrosine hydroxylase (TH) catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in the biosynthesis of dopamine. Recently, we described a point mutation in hTH (Q381K) in a family of two siblings suffering from progressive L-DOPA-responsive dystonia (DRD), representing the first reported mutation in this gene. We here describe the cloning, expression and steady-state...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Escherichia coli
Share to Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phenotype

Share to Point Mutation

Share to Polymerase Chain Reaction

Share to Recombinant Proteins

Share to Transcription, Genetic

Source

Identifiers

PMID: 8528210
DOI: 10.1093/hmg/4.7.1209

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene.PMID 8528210Read ↗

Tyrosine hydroxylase variants influence protein expression, cellular localization, stability, enzymatic activity and the physical interaction between tyrosine hydroxylase and GTP cyclohydrolase 1.Semantic proximity Read ↗

Biochemical and Molecular Genetic Characteristics of the Severe Form of Tyrosine Hydroxylase DeficiencySemantic proximity Read ↗

A novel compound heterozygous tyrosine hydroxylase mutation (p.R441P) with complex phenotype.Semantic proximity Read ↗

Dopamine inhibition of human tyrosine hydroxylase type 1 is controlled by the specific portion in the N-terminus of the enzyme.Semantic proximity Read ↗

Functional characterization of the S41Y (C2755A) polymorphism of tryptophan hydroxylase 2.Semantic proximity Read ↗

Tyrosine hydroxylase deficiency presenting with a biphasic clinical course.Semantic proximity Read ↗

Influence of human tryptophan hydroxylase 2 N- and C-terminus on enzymatic activity and oligomerization.Semantic proximity Read ↗

Genetics and biochemistry of dopa-responsive dystonia: significance of striatal tyrosine hydroxylase protein loss.Semantic proximity Read ↗

The V388M mutation results in a kinetic variant form of phenylalanine hydroxylase.Semantic proximity Read ↗

Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.Semantic proximity Read ↗

Characterization of wild-type and mutant forms of human tryptophan hydroxylase 2.Semantic proximity Read ↗

Partial characterization and three-dimensional-structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria.Semantic proximity Read ↗

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