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

Finnish-type aspartylglucosaminuria detected by oligonucleotide ligation assay.

Clinical chemistry - 1 Jan 1995

Delahunty C M, Ankener W, Brainerd S, Nickerson D A, Mononen I T

Abstract excerpt

Aspartylglycosaminuria (AGU) is a recessively inherited lysosomal storage disease that occurs with much higher frequency in Finland than elsewhere. AGU is caused by a deficiency in glycosylasparaginase (GA), which results in the accumulation of glycoasparagines in lysosomes. In the Finnish population, a single nucleotide change in the gene encoding GA is responsible for the disease. We have used the...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Base Sequence
Share to Heterozygote

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

Share to Homozygote

Share to Molecular Sequence Data

Share to Mutation

Share to Oligonucleotides

Share to Polymerase Chain Reaction

Source

Identifiers

PMID: 7813081

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

Finnish-type aspartylglucosaminuria detected by oligonucleotide ligation assay.PMID 7813081Read ↗

Oligonucleotide ligation assay: applications to molecular diagnosis of inherited disorders.Semantic proximity Read ↗

Convenient and quantitative determination of the frequency of a mutant allele using solid-phase minisequencing: application to aspartylglucosaminuria in Finland.Semantic proximity Read ↗

Genotyping by ligation assays.Semantic proximity Read ↗

Molecular diagnosis of medium-chain acyl-CoA dehydrogenase deficiency by oligonucleotide ligation assay.Semantic proximity Read ↗

Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.Semantic proximity Read ↗

Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.Semantic proximity Read ↗

Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.Semantic proximity Read ↗

Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease.Semantic proximity Read ↗

Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.Semantic proximity Read ↗

Determination of human NAT2 acetylator genotype by oligonucleotide ligation assay.Semantic proximity Read ↗

Automated DNA diagnostics using an ELISA-based oligonucleotide ligation assay.Semantic proximity Read ↗

Aspartylglycosaminuria: biochemistry and molecular biology.Semantic proximity Read ↗

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