Yeast prions: structure, biology, and prion-handling systems - Test2 - elhamkhani - TriplyDB

Yeast prions: structure, biology, and prion-handling systems

Yeast prions: structure, biology, and prion-handling systems

http://www.wikidata.org/entity/Q27007482

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Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease Molecular chaperones: guardians of the proteome in normal and disease states Disease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central Dogma More than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prions The Malignant Protein Puzzle.Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.Protein aggregation as a mechanism of adaptive cellular responses.Generating new prions by targeted mutation or segment duplication.The Human Disease-Associated Aβ Amyloid Core Sequence Forms Functional Amyloids in a Fungal Adhesin Prions are affected by evolution at two levels Controlling the prion propensity of glutamine/asparagine-rich proteins.DNA as information.Prion-specific Hsp40 function: The role of the auxilin homolog Swa2.Dual role of ribosome-associated chaperones in prion formation and propagation.The principle of conformational signaling.The "Jekyll and Hyde" Actions of Nucleic Acids on the Prion-like Aggregation of Proteins.Yeast and Fungal Prions.Prion-like proteins and their computational identification in proteomes.A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.Optimization of Aryl Amides that Extend Survival in Prion-Infected Mice.Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.Protein misfolding in Dictyostelium: Using a freak of nature to gain insight into a universal problem.The dominant-negative interplay between p53, p63 and p73: A family affair.Predicting Amyloidogenic Proteins in the Proteomes of Plants.Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III.Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field.Amyloid-Like β-Aggregates as Force-Sensitive Switches in Fungal Biofilms and Infections.Amyloids and prions in plants: Facts and perspectives.[PSI+] prion propagation is controlled by inositol polyphosphates.A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.Prion propagation and inositol polyphosphates.Nonsense-mediated mRNA decay factors cure most [PSI+] prion variants.Inter-Kingdom Modification of Metabolic Behavior: [GAR+] Prion Induction in Saccharomyces cerevisiae Mediated by Wine Ecosystem Bacteria

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P2860

Yeast prions: structure, biology, and prion-handling systems

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2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Yeast prions: structure, biology, and prion-handling systems

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Yeast prions: structure, biology, and prion-handling systems

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Microbiology and Molecular Biology Reviews

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Yeast prions: structure, biology, and prion-handling systems

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Anton Gorkovskiy

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David A. Bateman

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Evgeny E. Bezsonov

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Frank P. Shewmaker

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Herman K. Edskes

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Yaron Dayani

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P2860

Prion switching in response to environmental stress

Hook2 contributes to aggresome formation

Amyloid aggregates of the HET-s prion protein are infectious.

Yeast prions [URE3] and [PSI+] are diseases

Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae

Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor

The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae

Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast

Darwinian evolution of prions in cell culture

Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae

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10.1128/MMBR.00041-14

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1

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79

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25631286

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Prion protein family

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4402965

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