Search Results - "Chernova, Tatiana A."
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Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery
Published in Molecules (Basel, Switzerland) (18-09-2019)“…Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid…”
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Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements
Published in International journal of molecular sciences (12-05-2023)“…Prions are transmissible self-perpetuating protein isoforms associated with diseases and heritable traits. Yeast prions and non-transmissible protein…”
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Prion Induction by the Short-Lived, Stress-Induced Protein Lsb2 Is Regulated by Ubiquitination and Association with the Actin Cytoskeleton
Published in Molecular cell (22-07-2011)“…Yeast prions are self-perpetuating, QN-rich amyloids that control heritable traits and serve as a model for mammalian amyloidoses. De novo prion formation by…”
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Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress
Published in Cell reports (Cambridge) (17-01-2017)“…Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents…”
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Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association
Published in International journal of molecular sciences (16-07-2020)“…Yeast prions and mnemons are respectively transmissible and non-transmissible self-perpetuating protein assemblies, frequently based on cross-β ordered…”
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Profiling and verifying the substrates of E3 ubiquitin ligase Rsp5 in yeast cells
Published in STAR protocols (15-09-2023)“…Yeast is an essential model organism for studying protein ubiquitination pathways; however, identifying the direct substrates of E3 in the cell presents a…”
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Effects of Ubiquitin System Alterations on the Formation and Loss of a Yeast Prion
Published in The Journal of biological chemistry (02-02-2007)“…The yeast prion [PSI+] is a self-propagating amyloidogenic isoform of the translation termination factor Sup35. Overproduction of the chaperone protein Hsp104…”
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Prions, Chaperones, and Proteostasis in Yeast
Published in Cold Spring Harbor perspectives in biology (01-02-2017)“…Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of biological and pathological processes. Yeast prions are…”
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Pleiotropic Effects of Ubp6 Loss on Drug Sensitivities and Yeast Prion Are Due to Depletion of the Free Ubiquitin Pool
Published in The Journal of biological chemistry (26-12-2003)“…Mutation of the mouse Usp14 gene, encoding the homolog of yeast deubiquitinating enzyme Ubp6, causes ataxia. Here we show that deletion of the UBP6 gene in…”
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Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein
Published in Molecular microbiology (01-02-2000)“…Saccharomyces cerevisiae prion [PSI ] is a self‐propagating isoform of the eukaryotic release factor eRF3 (Sup35p). Sup35p consists of the evolutionary…”
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BRCA1-Associated Protein-1 Is a Tumor Suppressor that Requires Deubiquitinating Activity and Nuclear Localization
Published in Cancer research (Chicago, Ill.) (01-09-2008)“…BRCA1-associated protein-1 (BAP1), a deubiquitinating enzyme of unknown cellular function, is mutated in breast and lung cancers. In this study, we have shown…”
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Physiological and environmental control of yeast prions
Published in FEMS microbiology reviews (01-03-2014)“…Abstract Prions are self-perpetuating protein isoforms that cause fatal and incurable neurodegenerative disease in mammals. Recent evidence indicates that a…”
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Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer
Published in Cell chemical biology (16-09-2021)“…Attachment of the ubiquitin (UB) peptide to proteins via the E1-E2-E3 enzymatic machinery regulates diverse biological pathways, yet identification of the…”
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Distinct types of translation termination generate substrates for ribosome-associated quality control
Published in Nucleic acids research (19-08-2016)“…Cotranslational degradation of polypeptide nascent chains plays a critical role in quality control of protein synthesis and the rescue of stalled ribosomes. In…”
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Application of yeast to studying amyloid and prion diseases
Published in Advances in genetics (2020)“…Amyloids are fibrous cross-β protein aggregates that are capable of proliferation via nucleated polymerization. Amyloid conformation likely represents an…”
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To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1
Published in Molecular microbiology (01-07-2017)“…Summary Yeast self‐perpetuating protein aggregates (prions) provide a convenient model for studying various components of the cellular protein quality control…”
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Prion-based memory of heat stress in yeast
Published in Prion (04-05-2017)“…Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion…”
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Stress-dependent Proteolytic Processing of the Actin Assembly Protein Lsb1 Modulates a Yeast Prion
Published in The Journal of biological chemistry (03-10-2014)“…Yeast prions are self-propagating amyloid-like aggregates of Q/N-rich protein that confer heritable traits and provide a model of mammalian amyloidoses. [PSI+]…”
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Yeast studies reveal moonlighting functions of the ancient actin cytoskeleton
Published in IUBMB life (01-08-2014)“…Classic functions of the actin cytoskeleton include control of cell size and shape and the internal organization of cells. These functions are manifest in…”
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Hsp70 Chaperones as Modulators of Prion Life Cycle: Novel Effects of Ssa and Ssb on the Saccharomyces cerevisiae Prion [PSI+]
Published in Genetics (Austin) (01-03-2005)“…[PSI(+)] is a prion isoform of the yeast release factor Sup35. In some assays, the cytosolic chaperones Ssa1 and Ssb1/2 of the Hsp70 family were previously…”
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