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

Unraveling cellular phenotypes of novel TorsinA/TOR1A mutations.

Human mutation - 1 Sept 2014

Vulinovic Franca, Lohmann Katja, Rakovic Aleksandar, Capetian Philipp, Alvarez-Fischer Daniel, Schmidt Alexander, Weißbach Anne, Erogullari Alev, Kaiser Frank J, Wiegers Karin, Ferbert Andreas, Rolfs Arndt, Klein Christine, Seibler Philip

Abstract excerpt

A three-nucleotide (GAG) deletion (ΔE) in TorsinA (TOR1A) has been identified as the most common cause of dominantly inherited early-onset torsion dystonia (DYT1). TOR1A encodes a chaperone-like AAA+-protein localized in the endoplasmic reticulum. Currently, only three additional, likely mutations have been reported in single dystonia patients. Here, we report two new, putative TOR1A mutations (p.A14_P15del and...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy
Share to Dystonia Musculorum Deformans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intracellular Space

Share to Lysosomes

Share to Molecular Chaperones

Share to Protein Multimerization

Share to Protein Stability

Share to Proteolysis

Source

Identifiers

PMID: 24931141
DOI: 10.1002/humu.22604

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unraveling cellular phenotypes of novel TorsinA/TOR1A mutations.PMID 24931141Read ↗

Biochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1A.Semantic proximity Read ↗

Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells.Semantic proximity Read ↗

DYT-TOR1A dystonia: an update on pathogenesis and treatmentSemantic proximity Read ↗

The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Semantic proximity Read ↗

TorsinA and dystonia: from nuclear envelope to synapseSemantic proximity Read ↗

The role of torsinA in dystonia.Semantic proximity Read ↗

Consequences of the DYT1 mutation on torsinA oligomerization and degradation.Semantic proximity Read ↗

Inhibition of N-linked glycosylation prevents inclusion formation by the dystonia-related mutant form of torsinA.Semantic proximity Read ↗

Recombinant expression, purification, and comparative characterization of torsinA and its torsion dystonia-associated variant Delta E-torsinA.Semantic proximity Read ↗

Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia.Semantic proximity Read ↗

Effects of genetic variations in the dystonia protein torsinA: identification of polymorphism at residue 216 as protein modifier.Semantic proximity Read ↗

TorsinA and the torsinA-interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast.Semantic proximity Read ↗

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