2023
The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo
Grimes B, Jacob W, Liberman A, Kim N, Zhao X, Masison D, Greene L. The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo. Biomolecules 2023, 13: 1370. PMID: 37759770, PMCID: PMC10526957, DOI: 10.3390/biom13091370.Peer-Reviewed Original Research
2015
Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation
Malinovska L, Palm S, Gibson K, Verbavatz J, Alberti S. Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: e2620-e2629. PMID: 25941378, PMCID: PMC4443358, DOI: 10.1073/pnas.1504459112.Peer-Reviewed Original ResearchMeSH KeywordsDictyosteliumElectrophoresis, Polyacrylamide GelFluorescence Recovery After PhotobleachingHumansHuntingtin ProteinMicroscopy, ElectronMicroscopy, FluorescenceNerve Tissue ProteinsPeptide Termination FactorsPrionsProtein Aggregation, PathologicalProteomeProteostasis DeficienciesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsPrion-like proteinsD. discoideumMolecular chaperonesDictyostelium discoideumHuntingtin exon 1Yeast prion protein Sup35Prion-like domainsOverall aggregation propensityProtein-misfolding diseasesUbiquitin-proteasome systemPrion protein Sup35Rich proteomeHsp100 familyCellular proteostasisPrion stateCytosolic aggregatesSequence similarityPrion domainBioinformatics toolsProtein aggregationProteostatic capacityDiscoideumAggregation propensityProteomePrion protein
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