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

Mitochondrial membranes modify mutant huntingtin aggregation.

Biochimica et biophysica acta. Biomembranes - 1 Oct 2021

Adegbuyiro Adewale, Sedighi Faezeh, Jain Pranav, Pinti Mark V, Siriwardhana Chathuranga, Hollander John M, Legleiter Justin

Abstract excerpt

Huntington's disease (HD) is a neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. Expanded polyQ tracts are prone to aggregate into oligomers and insoluble fibrils. Mutant htt (mhtt) localizes to variety of organelles, including mitochondria. Specifically, mitochondrial defects, morphological alteration, and dysfunction are...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli
Share to Glutathione

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntingtin Protein

Share to Huntington Disease

Share to Mitochondrial Membranes

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 34089719
DOI: 10.1016/j.bbamem.2021.183663
PMCID: PMC8328955

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

Mitochondrial membranes modify mutant huntingtin aggregation.PMID 34089719Read ↗

Membranes as targets and modifiers of mutant huntingtin aggregation.Semantic proximity Read ↗

Structural insight into transmissive mutant huntingtin species by correlative light and electron microscopy and cryo-electron tomography.Semantic proximity Read ↗

Mutant huntingtin and mitochondrial dysfunction.Semantic proximity Read ↗

Lipid Composition Drives Mutant Huntingtin Dimerization and Membrane Association: Insights from Computational Simulations.Semantic proximity Read ↗

Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal PathologiesSemantic proximity Read ↗

Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.Semantic proximity Read ↗

Perturbation of the mitochondrial import machinery by aggregation prone Tau affects organelle morphology and reduces neuronal complexitySemantic proximity Read ↗

Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau proteinSemantic proximity Read ↗

Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons.Semantic proximity Read ↗

Aggregation and membrane activity of mutant A30P alpha-synuclein on mitochondrial membranes.Semantic proximity Read ↗

Alpha-synuclein fibrils induce budding of mitochondrial-derived vesiclesSemantic proximity Read ↗

Mitochondria "Shackled" by Mutant Huntingtin: Analysis of Morphological Alterations and Disruptions of Intracellular Transport.Semantic proximity Read ↗

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