Yeast prions: structure, biology, and prion-handling systems
about
Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseMolecular chaperones: guardians of the proteome in normal and disease statesDisease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central DogmaMore than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prionsThe 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 AdhesinPrions are affected by evolution at two levelsControlling 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
P2860
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P2860
Yeast prions: structure, biology, and prion-handling systems
description
2015 nî lūn-bûn
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2015 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի մարտին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Yeast prions: structure, biology, and prion-handling systems
@ast
Yeast prions: structure, biology, and prion-handling systems
@en
Yeast prions: structure, biology, and prion-handling systems
@nl
type
label
Yeast prions: structure, biology, and prion-handling systems
@ast
Yeast prions: structure, biology, and prion-handling systems
@en
Yeast prions: structure, biology, and prion-handling systems
@nl
prefLabel
Yeast prions: structure, biology, and prion-handling systems
@ast
Yeast prions: structure, biology, and prion-handling systems
@en
Yeast prions: structure, biology, and prion-handling systems
@nl
P2093
P2860
P356
P1476
Yeast prions: structure, biology, and prion-handling systems
@en
P2093
Anton Gorkovskiy
David A. Bateman
Evgeny E. Bezsonov
Frank P. Shewmaker
Herman K. Edskes
Yaron Dayani
P2860
P356
10.1128/MMBR.00041-14
P407
P50
P577
2015-03-01T00:00:00Z