Yeast chaperones and ubiquitin ligases contribute to proteostasis during arsenite stress by preventing or clearing protein aggregates

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Differential contributions of the proteasome, autophagy, and chaperones to the clearance of arsenite-induced protein aggregates in yeast

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Arsenite Binds to ZNF598 to Perturb Ribosome-Associated Protein Quality Control

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Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions

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Collided ribosomes form a unique structural interface to induce Hel2‐driven quality control pathways

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Targeted Degradation of Glucose Transporters Protects Against Arsenic Toxicity

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Ribosome Collision Is Critical for Quality Control during No-Go Decay

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Ubiquitination of stalled ribosome triggers ribosome-associated quality control

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Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

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Failure of RQC machinery causes protein aggregation and proteotoxic stress

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Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress

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Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility

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Not4-dependent translational repression is important for cellular protein homeostasis in yeast

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Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response

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Environmental pollutants as risk factors for neurodegenerative disorders: Alzheimer and Parkinson diseases

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The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress

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Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress

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Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress

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PolyQ Proteins Interfere with Nuclear Degradation of Cytosolic Proteins by Sequestering the Sis1p Chaperone

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Arsenic Binding to Proteins

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The ART-Rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress

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Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast

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Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates

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Trivalent Arsenic Inhibits the Functions of Chaperonin Complex

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Nascent Peptide-dependent Translation Arrest Leads to Not4p-mediated Protein Degradation by the Proteasome

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Arsenic(III) Species Inhibit Oxidative Protein Foldingin Vitro†

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