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

Aggregation of polyQ‐extended proteins is promoted by interaction with their natural coiled‐coil partners

11 Mar 2013

Abstract excerpt

Polyglutamine (polyQ) diseases are genetically inherited neurodegenerative disorders. They are caused by mutations that result in polyQ expansions of particular proteins. Mutant proteins form intranuclear aggregates, induce cytotoxicity and cause neuronal cell death. Protein interaction data suggest that polyQ regions modulate interactions between coiled-coil (CC) domains. In the case of the polyQ disease...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis Research
Share to Genetic Neurodegenerative Diseases
Share to Mitochondrial Function and Pathology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23483542
DOI: 10.1002/bies.201300001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aggregation of polyQ‐extended proteins is promoted by interaction with their natural coiled‐coil partnersPMID 23483542Read ↗

Identification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1.Semantic proximity Read ↗

Polyglutamine aggregation in Huntington and related diseases.Semantic proximity Read ↗

Identification of the ataxin-1 interaction network and its impact on spinocerebellar ataxia type 1Semantic proximity Read ↗

Opposing effects of polyglutamine expansion on native protein complexes contribute to SCA1.Semantic proximity Read ↗

The structural plasticity of polyglutamine repeatsSemantic proximity Read ↗

Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteinsSemantic proximity Read ↗

The Hsp40 co-chaperone DNAJC7 regulates polyglutamine aggregation and exhibits context-dependent effects on polyglycine aggregationSemantic proximity Read ↗

The polyglutamine protein ATXN2: from its molecular functions to its involvement in diseaseSemantic proximity Read ↗

ATAXIN-1 interacts with the repressor Capicua in its native complex to cause SCA1 neuropathology.Semantic proximity Read ↗

Juvenile Huntington’s Disease and Other PolyQ Diseases, Update on Neurodevelopmental Character and Comparative Bioinformatic Review of Transcriptomic and Proteomic DataSemantic proximity Read ↗

Pathogenic Mechanisms of a Polyglutamine-mediated Neurodegenerative Disease, Spinocerebellar Ataxia Type 1Semantic proximity Read ↗

Protein misfolding inside cells: The case of huntingtin and Huntington's diseaseSemantic proximity Read ↗

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