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

Aspartylglycosaminuria: a review.

Orphanet journal of rare diseases - 1 Dec 2016

Arvio Maria, Mononen Ilkka

Abstract excerpt

Aspartylglucosaminuria (AGU), a recessively inherited lysosomal storage disease, is the most common disorder of glycoprotein degradation with a high prevalence in the Finnish population. It is a lifelong condition affecting on the patient's appearance, cognition, adaptive skills, physical growth, personality, body structure, and health. An infantile growth spurt and development of macrocephalia associated to...

Read the complete abstract on PubMed

Topics

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

Share to Glycoproteins
Share to Lysosomal Storage Diseases
Share to Acetylglucosamine

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

Share to Cellular transport and secretion

Share to AGA gene

Share to Glycogen Storage Diseases and Myoclonus

Share to Lysosomal Storage Disorders Research

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 27906067
DOI: 10.1186/s13023-016-0544-6
PMCID: PMC5134220

Genes

AGA

Variants

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

Aspartylglycosaminuria: a review.PMID 27906067Read ↗

Aspartylglycosaminuria: biochemistry and molecular biology.Semantic proximity Read ↗

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

A mouse model for the human lysosomal disease aspartylglycosaminuriaSemantic proximity Read ↗

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

Phenotypic characterization of mice with targeted disruption of glycosylasparaginase gene: a mouse model for aspartylglycosaminuria.Semantic proximity Read ↗

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

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

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

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

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

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