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

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.

Scientific reports - 22 Jun 2018

Zhao Yanding, Zurawel Ashley A, Jenkins Nicole P, Duennwald Martin L, Cheng Chao, Kettenbach Arminja N, Supattapone Surachai

Abstract excerpt

Huntington's disease is caused by the pathological expansion of a polyglutamine (polyQ) stretch in Huntingtin (Htt), but the molecular mechanisms by which polyQ expansion in Htt causes toxicity in selective neuronal populations remain poorly understood. Interestingly, heterologous expression of expanded polyQ Htt is toxic in Saccharomyces cerevisiae cells, but has no effect in Schizosaccharomyces pombe, a related...

Read the complete abstract on PubMed

Topics

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

Share to Computational Biology
Share to Huntingtin Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptides

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Schizosaccharomyces

Share to Schizosaccharomyces pombe Proteins

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 29934597
DOI: 10.1038/s41598-018-27900-5
PMCID: PMC6015068

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.PMID 29934597Read ↗

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

Mutant Huntingtin Protein Interaction Map Implicates Dysregulation of Multiple Cellular Pathways in Neurodegeneration of Huntington’s DiseaseSemantic proximity Read ↗

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

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

Differential effects of soluble and aggregating polyQ proteins on cytotoxicity and type-1 myosin-dependent endocytosis in yeast.Semantic proximity Read ↗

Polyglutamine toxicity in yeast uncovers phenotypic variations between different fluorescent protein fusions.Semantic proximity Read ↗

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

Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors.Semantic proximity Read ↗

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

HAP40 is a conserved central regulator of Huntingtin and a specific modulator of mutant Huntingtin toxicitySemantic proximity Read ↗

Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in Saccharomyces cerevisiaeSemantic proximity Read ↗

Recent Advances in the Study of Huntingtin Interacting ProteinsSemantic proximity Read ↗

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