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

The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome.

Proceedings of the National Academy of Sciences of the United States of America - 13 May 2003

Cronshaw Janet M, Matunis Michael J

Abstract excerpt

Triple A syndrome is a human autosomal recessive disorder characterized by an unusual array of tissue-specific defects. Triple A syndrome arises from mutations in a WD-repeat protein of unknown function called ALADIN (also termed Adracalin or AAAS). We showed previously that ALADIN localizes to nuclear pore complexes (NPCs), large multiprotein assemblies that are the sole sites of nucleocytoplasmic transport....

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Adrenal Insufficiency

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Esophageal Achalasia

Share to Genes, Recessive

Share to HeLa Cells

Share to Hypoglycemia

Share to Nuclear Pore

Share to Nuclear Pore Complex Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 12730363
DOI: 10.1073/pnas.1031047100
PMCID: PMC156285

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome.PMID 12730363Read ↗

The triple A syndrome is due to mutations in ALADIN, a novel member of the nuclear pore complex.Semantic proximity Read ↗

Triple-A Syndrome (TAS): An In-Depth Overview on Genetic and Phenotype Heterogeneity.Semantic proximity Read ↗

Biallelic NDC1 variants that interfere with ALADIN binding are associated with neuropathy and triple A-like syndrome.Semantic proximity Read ↗

Cellular localization of 17 natural mutant variants of ALADIN protein in triple A syndrome - shedding light on an unexpected splice mutation.Semantic proximity Read ↗

ALADINI482S causes selective failure of nuclear protein import and hypersensitivity to oxidative stress in triple A syndrome.Semantic proximity Read ↗

Triple A syndrome is caused by mutations in AAAS, a new WD-repeat protein gene.Semantic proximity Read ↗

COMPENSATION FOR CHRONIC OXIDATIVE STRESS IN ALADIN NULL MICESemantic proximity Read ↗

Mutation of the nuclear pore complex component, aladin1, disrupts asymmetric cell division in Zea mays (maize).Semantic proximity Read ↗

Clinical and genetic characterisation of a series of patients with triple A syndrome.Semantic proximity Read ↗

ATAD3A: A Key Regulator of Mitochondria-Associated Diseases.Semantic proximity Read ↗

New insights into the molecular basis of the triple A syndrome.Semantic proximity Read ↗

Mutation of the nuclear pore complex component, <i>aladin1</i> , disrupts asymmetric cell division in <i>Zea mays</i> (maize)Semantic proximity Read ↗

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