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

Inhibition of transglutaminase exacerbates polyglutamine-induced neurotoxicity by increasing the aggregation of mutant ataxin-3 in an SCA3 Drosophila model.

Neurotoxicity research - 1 Apr 2015

Lin Yunting, He Hua, Luo Yingying, Zhu Ting, Duan Ranhui

Abstract excerpt

Transglutaminases (TGs) comprise a family of Ca(2+)-dependent enzymes that catalyze protein cross-linking, which include nine family members in humans but only a single homolog in Drosophila with three conserved domains. Drosophila Tg plays important roles in cuticle morphogenesis, hemolymph clotting, and innate immunity. Mammalian tissue TG (TG2) is involved in polyglutamine diseases (polyQ diseases), and TG6...

Read the complete abstract on PubMed

Topics

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

Share to Ataxin-3
Share to Disease Models, Animal

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

Share to Drosophila

Share to Gene Knockdown Techniques

Share to Mutation

Share to Peptides

Share to Spinocerebellar Ataxias

Share to Transglutaminases

Source

Identifiers

PMID: 25501875
DOI: 10.1007/s12640-014-9506-8

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

Inhibition of transglutaminase exacerbates polyglutamine-induced neurotoxicity by increasing the aggregation of mutant ataxin-3 in an SCA3 Drosophila model.PMID 25501875Read ↗

Machado–Joseph disease/spinocerebellar ataxia type 3: lessons from disease pathogenesis and clues into therapySemantic proximity Read ↗

Large-Scale Screen for Modifiers of Ataxin-3-Derived Polyglutamine-Induced Toxicity in DrosophilaSemantic proximity Read ↗

Polyglutamine-induced neurodegeneration in SCA3 is not mitigated by non-expanded ataxin-3: conclusions from double-transgenic mouse models.Semantic proximity Read ↗

Protein crosslinking by transglutaminase controls cuticle morphogenesis in Drosophila.Semantic proximity Read ↗

Polyglutamine diseases: The special case of ataxin-3 and Machado–Joseph diseaseSemantic proximity Read ↗

Targeting the VCP-binding motif of ataxin-3 improves phenotypes in Drosophila models of Spinocerebellar Ataxia Type 3.Semantic proximity Read ↗

T1-11 and JMF1907 ameliorate polyglutamine-expanded ataxin-3-induced neurodegeneration, transcriptional dysregulation and ataxic symptom in the SCA3 transgenic mouseSemantic proximity Read ↗

Mutant Ataxin-3-Containing Aggregates (MATAGGs) in Spinocerebellar Ataxia Type 3: Dynamics of the Disorder.Semantic proximity Read ↗

Identification of genes that modify ataxin-1-induced neurodegeneration.Semantic proximity Read ↗

Sodium valproate alleviates neurodegeneration in SCA3/MJD via suppressing apoptosis and rescuing the hypoacetylation levels of histone H3 and H4.Semantic proximity Read ↗

A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila.Semantic proximity Read ↗

N-terminal ataxin-3 causes neurological symptoms with inclusions, endoplasmic reticulum stress and ribosomal dislocation.Semantic proximity Read ↗

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