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

Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease.

Human molecular genetics - 1 Jun 2001

Sittler A, Lurz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl M K, Hartl F U, Wanker E E

Abstract excerpt

Huntington's disease (HD) is a progressive neurodegenerative disorder with no effective treatment. Geldanamycin is a benzoquinone ansamycin that binds to the heat shock protein Hsp90 and activates a heat shock response in mammalian cells. In this study, we show by using a filter retardation assay and immunofluorescence microscopy that treatment of mammalian cells with geldanamycin at nanomolar concentrations...

Read the complete abstract on PubMed

Topics

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

Share to Benzoquinones
Share to Heat-Shock Response

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP40 Heat-Shock Proteins

Share to HSP70 Heat-Shock Proteins

Share to HSP90 Heat-Shock Proteins

Share to Huntingtin Protein

Share to Lactams, Macrocyclic

Share to Quinones

Source

Identifiers

PMID: 11406612
DOI: 10.1093/hmg/10.12.1307

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

Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease.PMID 11406612Read ↗

A Filter Retardation Assay Facilitates the Detection and Quantification of Heat-Stable, Amyloidogenic Mutant Huntingtin Aggregates in Complex Biosamples.Semantic proximity Read ↗

Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assaySemantic proximity Read ↗

A Novel Hsp90 Inhibitor Activates Compensatory Heat Shock Protein Responses and Autophagy and Alleviates Mutant A53T α-Synuclein Toxicity.Semantic proximity Read ↗

Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease.Semantic proximity Read ↗

Azadiradione regulates Heat Shock Factor 1 function by interacting with its DNA-binding domain independent of the oligomerization domainSemantic proximity Read ↗

Alleviating neurodegeneration by an anticancer agent: an Hsp90 inhibitor (17-AAG).Semantic proximity Read ↗

Redefining the Phenotype of Heat Shock Protein 90 (Hsp90) Inhibitors.Semantic proximity Read ↗

Inhibition of Aggregation of Mutant Huntingtin by Nucleic Acid Aptamers In Vitro and in a Yeast Model of Huntington's Disease.Semantic proximity Read ↗

Mechanistic studies on Hsp90 inhibition by ansamycin derivatives.Semantic proximity Read ↗

The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin.Semantic proximity Read ↗

Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models.Semantic proximity Read ↗

Geldanamycin and its derivatives as Hsp90 inhibitors.Semantic proximity Read ↗

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