<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Albakri MB</submitter><funding>The University of Western Ontario</funding><funding>Canadian Institutes of Health Research</funding><funding>CIHR</funding><pagination>1242</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6290977</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>7</volume><pubmed_abstract>Development of fluorescent proteins (FPs) enabled researchers to visualize protein localization and trafficking in living cells and organisms. The extended palette of available FPs allows simultaneous detection of multiple fluorescent fusion proteins. Importantly, FPs are originally derived from different organisms from jelly fish to corals and each FP displays its own biophysical properties. Among these properties, the tendency of FPs to oligomerize inherently affects the behavior of its fusion partner. Here we employed the budding yeast &lt;i>Saccharomyces cerevisiae&lt;/i> to determine the impact of the latest generation of red FPs on their binding partner. We used a yeast assay based on the aggregation and toxicity of misfolded polyQ expansion proteins linked to Huntington's disease. Since p</pubmed_abstract><journal>F1000Research</journal><pubmed_title>Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in &lt;i>Saccharomyces cerevisiae&lt;/i>.</pubmed_title><pmcid>PMC6290977</pmcid><funding_grant_id>MOP-325538</funding_grant_id><pubmed_authors>Jiang Y</pubmed_authors><pubmed_authors>Lajoie P</pubmed_authors><pubmed_authors>Genereaux J</pubmed_authors><pubmed_authors>Albakri MB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in &lt;i>Saccharomyces cerevisiae&lt;/i>.</name><description>Development of fluorescent proteins (FPs) enabled researchers to visualize protein localization and trafficking in living cells and organisms. The extended palette of available FPs allows simultaneous detection of multiple fluorescent fusion proteins. Importantly, FPs are originally derived from different organisms from jelly fish to corals and each FP displays its own biophysical properties. Among these properties, the tendency of FPs to oligomerize inherently affects the behavior of its fusion partner. Here we employed the budding yeast &lt;i>Saccharomyces cerevisiae&lt;/i> to determine the impact of the latest generation of red FPs on their binding partner. We used a yeast assay based on the aggregation and toxicity of misfolded polyQ expansion proteins linked to Huntington's disease. Since p</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018</publication><modification>2026-04-08T04:35:30.494Z</modification><creation>2019-03-26T22:36:43Z</creation></dates><accession>S-EPMC6290977</accession><cross_references><pubmed>30631438</pubmed><doi>10.12688/f1000research.15829.2</doi></cross_references></HashMap>