First-pass extracted concept

polyglutamine proteins

Candidate: concept label1 source documents5 linked claims

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Aliases

polyQ peptides, polyQ proteins

Extracted Explainers

What the tool is doing

This label refers to proteins or peptides containing expanded polyglutamine tracts that are discussed as undergoing conformational change, oligomerisation, and aggregation.

Source 1DOI PubMed

What problem it solves

It provides the central mechanistic category for comparing monomeric conformations, oligomeric intermediates, and aggregate states across polyQ diseases.

Source 1DOI PubMed

What it does not solve

It is not itself a discrete experimental tool or engineered construct.

Source 1DOI PubMed

Evidence Snippets

Here, we review what is known about conformations of polyQ peptides and proteins in their monomeric state from experimental and modelling data, how conformational changes of polyQ proteins relate to their oligomerisation and morphology of aggregates...

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1review2010Acta NeuropathologicaDOI PubMed

1 evidence snippet 5 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1associationsupports2010Source 1DOI PubMed

Polyglutamine diseases are associated with CAG/polyQ expansion mutations in unrelated proteins, and elongation of the glutamine tract is associated with intracellular aggregation and neurotoxicity mainly in the CNS.

Quoted textsource-backed

Polyglutamine (polyQ) diseases are associated with a CAG/polyQ expansion mutation in unrelated proteins. Upon elongation of the glutamine tract, disease proteins aggregate within cells, mainly in the central nervous system (CNS) and this aggregation process is associated with neurotoxicity.

Claim 2knowledge gapneutral2010Source 1DOI PubMed

It remains unclear to what extent and by what mechanisms polyQ aggregation causes neuronal dysfunction in the CNS.

Quoted textsource-backed

However, it remains unclear to what extent and how this aggregation causes neuronal dysfunction in the CNS.

Claim 3mechanistic hypothesissupports2010Source 1DOI PubMed

PolyQ expansion-induced conformational changes and surrounding sequence context may drive formation of particular oligomeric intermediates with differential neurotoxicity.

Quoted textsource-backed

Initial evidence suggests that conformational changes induced by polyQ expansions and their surrounding sequence lead to the formation of particular oligomeric intermediates that may differentially affect neurotoxicity.

Claim 4mechanistic summarysupports2010Source 1DOI PubMed

Conformational changes of polyQ proteins relate to oligomerisation, aggregate morphology, and impaired cellular functions in vitro and in vivo.

Quoted textsource-backed

Here, we review what is known about conformations of polyQ peptides and proteins in their monomeric state from experimental and modelling data, how conformational changes of polyQ proteins relate to their oligomerisation and morphology of aggregates and which cellular function are impaired by oligomers, in vitro and in vivo.

Claim 5modulationsupports2010Source 1DOI PubMed

Cellular mechanisms and co-factors can modulate the folding pathway and kinetics of polyQ aggregation.

Quoted textsource-backed

We also summarise the key modulatory cellular mechanisms and co-factors, which could affect the folding pathway and kinetics of polyQ aggregation.