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

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

Proceedings of the National Academy of Sciences of the United States of America - 14 Feb 2006

Hirano Makito, Furiya Yoshiko, Asai Hirohide, Yasui Akira, Ueno Satoshi

Abstract excerpt

Triple A syndrome is an autosomal recessive neuroendocrinological disease caused by mutations in a gene that encodes 546 amino acid residues. The encoded protein is the nucleoporin ALADIN, a component of nuclear pore complex (NPC). We identified a mutant ALADIN(I482S) that fails to target NPC and investigated the consequences of mistargeting using cultured fibroblasts (I482Sf) from a patient with triple A...

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to Active Transport, Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Repair Enzymes

Share to Endocrine System Diseases

Share to Nervous System Diseases

Share to Nuclear Pore

Share to Nuclear Pore Complex Proteins

Share to Oxidative Stress

Source

Open in PubMed Open full text

Identifiers

PMID: 16467144
DOI: 10.1073/pnas.0505598103
PMCID: PMC1413683

Genes

APTX

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

ALADINI482S causes selective failure of nuclear protein import and hypersensitivity to oxidative stress in triple A syndrome.PMID 16467144Read ↗

The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome.Semantic proximity Read ↗

COMPENSATION FOR CHRONIC OXIDATIVE STRESS IN ALADIN NULL MICESemantic 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 ↗

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 ↗

Triple A syndrome in Japan.Semantic proximity Read ↗

A-type lamins: guardians of the soma?Semantic proximity Read ↗

Dominant-negative NARS1 R534∗ mutation causes wild-type subunit poisoning and heterodimer predominance in cellsSemantic proximity Read ↗

Mis-regulation of the Nucleoporins 98 and 96 lead to defects in protein synthesis that promote hallmarks of tumorigenesisSemantic proximity Read ↗

A bipartite, mutation-tolerant NLS regulates interaction of ΔNp63α with importin alpha, nuclear transport and transcriptional activitySemantic proximity Read ↗

Silencing nuclear pore protein Tpr elicits a senescent-like phenotype in cancer cells.Semantic proximity Read ↗

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