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

Rapamycin alleviates toxicity of different aggregate-prone proteins.

Human molecular genetics - 1 Feb 2006

Berger Zdenek, Ravikumar Brinda, Menzies Fiona M, Oroz Lourdes Garcia, Underwood Benjamin R, Pangalos Menelas N, Schmitt Ina, Wullner Ullrich, Evert Bernd O, O'Kane Cahir J, Rubinsztein David C

Abstract excerpt

Many neurodegenerative diseases are caused by intracellular, aggregate-prone proteins, including polyglutamine-expanded huntingtin in Huntington's disease (HD) and mutant tau in fronto-temporal dementia/tauopathy. Previously, we showed that rapamycin, an autophagy inducer, enhances mutant hunting...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy
Share to Chlorocebus aethiops
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntington Disease

Share to Protein Structure, Quaternary

Share to Sirolimus

Share to tau Proteins

Share to Trinucleotide Repeat Expansion

Source

Identifiers

PMID: 16368705
DOI: 10.1093/hmg/ddi458

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16368705-2026-09-02.1. Manifest publication-graph-cohort-2026-09-02.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rapamycin alleviates toxicity of different aggregate-prone proteins.PMID 16368705Read ↗

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease.Semantic proximity Read ↗

Chemical inducers of autophagy that enhance the clearance of mutant proteins in neurodegenerative diseases.Semantic proximity Read ↗

Autophagy in neurodegeneration and developmentSemantic proximity Read ↗

Role of autophagy in the clearance of mutant huntingtin: a step towards therapy?Semantic proximity Read ↗

Drosophila melanogaster as a model to study autophagy in neurodegenerative diseases induced by proteinopathiesSemantic proximity Read ↗

Huntington's disease: degradation of mutant huntingtin by autophagy.Semantic proximity Read ↗

Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies.Semantic proximity Read ↗

Therapeutic induction of autophagy to modulate neurodegenerative disease progressionSemantic proximity Read ↗

Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy.Semantic proximity Read ↗

Rapamycin alleviates pathogenesis of a new Drosophila model of ALS-TDP.Semantic proximity Read ↗

Targeting autophagy in ALS: a complex mission.Semantic proximity Read ↗

Autophagy activation ameliorates neuronal pathogenesis of FTLD-U miceSemantic proximity Read ↗

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