Polyglutamine Expansion
Polyglutamine Expansion - Related Videos
09:06
Growth Assays to Assess Polyglutamine Toxicity in Yeast
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Cited by 3 •
2012
This manuscript describes three complementary protocols for assessing the toxicity of polyglutamine (polyQ)-expansion proteins in the yeast Saccharomyces cerevisiae. These protocols can easily be modified to monitor the toxicity of other misfolded proteins in yeast.
09:42
Analysis of Thermal Expansion via Dilatometry
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2023
Source: J. Jacob Chavez, Ryan T. Davis, and Taylor D. Sparks, Department of Materials Science and Engineering, The University of Utah, Salt Lake City, UT Thermal expansion is extremely important when considering which materials will be used in systems that experience fluctuations in temperature. A high or low thermal expansion in a material may or may not be desirable, depending on the application. For instance, in a common liquid thermometer, a material with a high thermal expansion would be...
03:03
Fluorescent Reporter-Based Paralysis Assay: A Technique to Assess Age-Associated Progressive Formation of Polyglutamine Fluorescent Reporter and Associated Paralysis in Caenorhabditis elegans
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2025
This video demonstrates an in vivo imaging-based assay to determine proteostasis decline due to aging. The assay uses Caenorhabditis elegans expressing polyglutamine YFP-fusion protein in body wall muscles to measure the age-associated aggregation of polyglutamine and induction of proteotoxicity, leading to paralysis.
09:23
Effect of Fluorescent Proteins on Fusion Partners Using Polyglutamine Toxicity Assays in Yeast
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Cited by 1 •
2018
This article describes protocols to assess the effect of fluorescent proteins on the aggregation and toxicity of misfolded polyglutamine expansion for the rapid evaluation of a newly uncharacterized fluorescent protein in the context of fluorescent reporters.
01:24
Heat and Free Expansion
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2023
The work done by a thermodynamic system depends not only on the initial and final states but also on the intermediate states—that is, on the path. Like work, when heat is added to a thermodynamic system, it undergoes a change of state, and the state attained depends on the path from the initial state to the final state. Consider an ideal gas cylinder fitted with a piston. When the cylinder is heated at a constant temperature, the gas molecules absorb energy and expand slowly in a controlled...
FAQs
An expanded tract does not have one universal pathogenic cutoff: its significance depends on a disease-specific threshold. Crossing that threshold is associated with increased risk that the protein will misfold, aggregate inside cells, and interfere with cellular pathways. Comparing tract length with the relevant threshold therefore helps connect a molecular alteration to disease onset and inherited disorder patterns.
Polyglutamine expansion can alter several linked protein properties rather than producing a single defect. The longer glutamine tract may affect folding, stability, molecular interactions, and degradation. These changes can promote misfolded protein accumulation and intracellular aggregate formation, giving biochemical studies multiple endpoints for evaluating how the altered protein disrupts neuronal function.
Its importance extends beyond identifying an altered protein. Biochemical study connects the expanded tract with changes in folding, stability, interactions, degradation, and aggregate formation, then relates those disturbances to impaired cellular pathways and neuronal function. This framework helps researchers investigate why particular tissues may be especially affected without treating aggregation as the only relevant mechanism.
Repeat instability is a direct research target because changes in the repeat can be considered alongside the resulting protein abnormalities. Investigating it may help clarify how the molecular change relates to disease onset and inheritance patterns. It also provides one possible intervention point, alongside aggregation and impaired clearance, for developing therapeutic strategies.
Biochemical studies can support biomarker development by linking repeat-associated protein changes to measurable indicators of disease-related biology. The source places biomarkers alongside investigations of repeat instability, aggregation, and impaired clearance as research outcomes. Such markers could help connect molecular mechanisms with therapeutic development, although the specific biomarker type is not defined here.
Three intervention points are highlighted: repeat instability, protein aggregation, and impaired clearance. Targeting these processes addresses different aspects of the problem, from the underlying repeat change to the accumulation or removal of abnormal protein. Comparing these targets can help organize therapeutic research around molecular cause, cellular consequence, and protein handling.