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

N-acetylglutamate synthase deficiency and the treatment of hyperammonemic encephalopathy.

Annals of neurology - 1 Dec 2002

Elpeleg Orly, Shaag Avraham, Ben-Shalom Efrat, Schmid Tal, Bachmann Claude

Abstract excerpt

Carbamylphosphate synthase is the first enzymatic reaction of the urea cycle. Its activator, N-acetylglutamate, is synthesized from acetyl-CoA and glutamate in a reaction catalyzed by N-acetylglutamate synthase (NAGS). We have identified the putative human NAGS gene and report the first mutation in this gene in a family with carbamylglutamate responsive hyperammonemia and normal activity of the urea cycle...

Read the complete abstract on PubMed

Topics

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

Share to Acetyltransferases
Share to Amino Acid Sequence
Share to Brain Diseases, Metabolic, Inborn

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Child, Preschool

Share to Glutamates

Share to Hyperammonemia

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 12447942
DOI: 10.1002/ana.10406

Genes

NAGS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

N-acetylglutamate synthase deficiency and the treatment of hyperammonemic encephalopathy.PMID 12447942Read ↗

Mutations and polymorphisms in the human N-acetylglutamate synthase (NAGS) gene.Semantic proximity Read ↗

N-acetylglutamate synthase deficiency: Novel mutation associated with neonatal presentation and literature review of molecular and phenotypic spectraSemantic proximity Read ↗

Mutation analysis in patients with N-acetylglutamate synthase deficiency.Semantic proximity Read ↗

N-carbamylglutamate enhancement of ureagenesis leads to discovery of a novel deleterious mutation in a newly defined enhancer of the NAGS gene and to effective therapy.Semantic proximity Read ↗

Null mutations in the N-acetylglutamate synthase gene associated with acute neonatal disease and hyperammonemia.Semantic proximity Read ↗

Impaired ureagenesis due to arginine-insensitive N-acetylglutamate synthaseSemantic proximity Read ↗

Mammalian N-acetylglutamate synthase.Semantic proximity Read ↗

Understanding N-Acetyl-L-Glutamate Synthase Deficiency: Mutational Spectrum, Impact of Clinical Mutations on Enzyme Functionality, and Structural Considerations.Semantic proximity Read ↗

Favourable long-term outcome after immediate treatment of neonatal hyperammonemia due to N-acetylglutamate synthase deficiency.Semantic proximity Read ↗

Targeting CPS1 in the treatment of Carbamoyl phosphate synthetase 1 (CPS1) deficiency, a urea cycle disorder.Semantic proximity Read ↗

Late onset N-acetylglutamate synthase deficiency caused by hypomorphic alleles.Semantic proximity Read ↗

Non-coding sequence variants define a novel regulatory element in the first intron of the N-acetylglutamate synthase gene.Semantic proximity Read ↗

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