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

Sir2 is induced by oxidative stress in a yeast model of Huntington disease and its activation reduces protein aggregation.

Archives of biochemistry and biophysics - 1 Jun 2011

Sorolla M Alba, Nierga Clara, Rodríguez-Colman M José, Reverter-Branchat Gemma, Arenas Alicia, Tamarit Jordi, Ros Joaquim, Cabiscol Elisa

Abstract excerpt

Huntington disease (HD) is a neurodegenerative disorder caused by expansion of CAG trinucleotide repeats, leading to an elongated polyglutamine sequence (polyQ) in the huntingtin protein. Misfolding of mutant polyQ proteins with expanded tracts results in aggregation, causing cytotoxicity. Oxidative stress in HD has been documented in humans as important to disease progression. Using yeast cells as a model of HD,...

Read the complete abstract on PubMed

Topics

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

Share to Huntington Disease
Share to Mutant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Niacinamide

Share to Oxidative Stress

Share to Peptides

Share to Saccharomyces cerevisiae

Share to Silent Information Regulator Proteins, Saccharomyces cerevisiae

Share to Sirtuin 2

Source

Identifiers

PMID: 21513696
DOI: 10.1016/j.abb.2011.04.002

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

Sir2 is induced by oxidative stress in a yeast model of Huntington disease and its activation reduces protein aggregation.PMID 21513696Read ↗

Growth assays to assess polyglutamine toxicity in yeast.Semantic proximity Read ↗

Protein aggregation and neurodegeneration: clues from a yeast model of Huntington's disease.Semantic proximity Read ↗

Expression of an expanded polyglutamine domain in yeast causes death with apoptotic markers.Semantic proximity Read ↗

From the Bakery to the Brain Business: Developing Inducible Yeast Models of Human Neurodegenerative DisordersSemantic proximity Read ↗

Exploiting yeast genetics to inform therapeutic strategies for Huntington's disease.Semantic proximity Read ↗

Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.Semantic proximity Read ↗

Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity.Semantic proximity Read ↗

Protein oxidation in Huntington disease.Semantic proximity Read ↗

Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1.Semantic proximity Read ↗

Protein aggregation activates erratic stress response in dietary restricted yeast cells.Semantic proximity Read ↗

Biphasic Temporal Remodeling Of The Proteome In A Polyglutamine-Expanded Huntingtin In Vitro Aggregation Cell Model: From Early Rna-Regulatory Compensation To Selective Mitochondrial Energy FailureSemantic proximity Read ↗

Cytotoxicity of mutant huntingtin fragment in yeast can be modulated by the expression level of wild type huntingtin fragment.Semantic proximity Read ↗

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