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

Disruption of Protein Processing in the Endoplasmic Reticulum of DYT1 Knock-in Mice Implicates Novel Pathways in Dystonia Pathogenesis.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 5 Oct 2016

Beauvais Genevieve, Bode Nicole M, Watson Jaime L, Wen Hsiang, Glenn Kevin A, Kawano Hiroyuki, Harata N Charles, Ehrlich Michelle E, Gonzalez-Alegre Pedro

Abstract excerpt

Dystonia type 1 (DYT1) is a dominantly inherited neurological disease caused by mutations in TOR1A, the gene encoding the endoplasmic reticulum (ER)-resident protein torsinA. Previous work mostly completed in cell-based systems suggests that mutant torsinA alters protein processing in the secretory pathway. We hypothesized that inducing ER stress in the mammalian brain in vivo would trigger or exacerbate mutant...

Read the complete abstract on PubMed

Topics

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

Share to Calcium Signaling
Share to Cerebellum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dystonia

Share to Endoplasmic Reticulum

Share to Endoplasmic Reticulum Stress

Share to Gene Knock-In Techniques

Share to HSP40 Heat-Shock Proteins

Share to Molecular Chaperones

Source

Open in PubMed Open full text

Identifiers

PMID: 27707963
DOI: 10.1523/JNEUROSCI.0669-16.2016
PMCID: PMC5050323

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disruption of Protein Processing in the Endoplasmic Reticulum of DYT1 Knock-in Mice Implicates Novel Pathways in Dystonia Pathogenesis.PMID 27707963Read ↗

DYT-TOR1A Subcellular Proteomics Reveals Selective Vulnerability of the Nuclear Proteome to Cell StressSemantic proximity Read ↗

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

The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress responseSemantic proximity Read ↗

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

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

Developments in the molecular biology of DYT1 dystonia.Semantic proximity Read ↗

The zebrafish homologue of the human DYT1 dystonia gene is widely expressed in CNS neurons but non-essential for early motor system development.Semantic proximity Read ↗

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

The role of torsinA in dystonia.Semantic 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 ↗

Mislocalization to the nuclear envelope: an effect of the dystonia-causing torsinA mutation.Semantic proximity Read ↗

Mutations in THAP1/DYT6 reveal that diverse dystonia genes disrupt similar neuronal pathways and functions.Semantic proximity Read ↗

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