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Article

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

Scandinavian journal of clinical and laboratory investigation. Supplementum - 1 Jan 1993

Ikonen E, Syvänen A C, Peltonen L

Abstract excerpt

Aspartylglucosaminuria (AGU) is exceptional among lysosomal storage diseases since it represents the only known amidase deficiency in man, being caused by an inadequate function of aspartylglucosaminidase (AGA, E.C. 3.5.1.26.). This amidase is essential in one of the final steps in the ordered breakdown of glycoproteins since it cleaves Asn from the residual N-acetylglucosamines (for reviews see 1, 2). The...

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Source

Identifiers

PMID: 8322015
DOI: 10.3109/00365519309090670

Genes

AGA

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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.PMID 8322015Read ↗

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

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

Aspartylglycosaminuria: biochemistry and molecular biology.Semantic proximity Read ↗

Aspartylglucosaminuria caused by a novel homozygous mutation in the AGA gene was identified by an exome-first approach in a patient from Japan.Semantic proximity Read ↗

Aspartylglycosaminuria: a review.Semantic proximity Read ↗

Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation.Semantic proximity Read ↗

Validation of Aspartylglucosaminidase Activity Assay for Human Serum Samples: Establishment of a Biomarker for Diagnostics and Clinical StudiesSemantic proximity Read ↗

Aspartylglucosaminuria (AGU): protein and gene structure of normal and mutated aspartylglucosaminidase.Semantic proximity Read ↗

Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.Semantic proximity Read ↗

Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients.Semantic proximity Read ↗

[A family with two children diagnosed with aspartylglucosaminuria-case report and literature review].Semantic proximity Read ↗

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

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