about
Prion hypothesis: the end of the controversy?Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentationPrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseMore than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prionsActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastPotential roles for prions and protein-only inheritance in cancerYeast prions: structure, biology, and prion-handling systemsA novel single-cell screening platform reveals proteome plasticity during yeast stress responsesRebels with a cause: molecular features and physiological consequences of yeast prionsConformational analysis of misfolded protein aggregation by FRET and live-cell imaging techniquesEngineering enhanced protein disaggregases for neurodegenerative diseaseAmyloid-associated activity contributes to the severity and toxicity of a prion phenotypeDisentangling genetic and epigenetic determinants of ultrafast adaptationNon-genetic individuality in Escherichia coli motor switching.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.High-resolution structure of infectious prion protein: the final frontierUse of yeast as a system to study amyloid toxicity[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Luminidependens (LD) is an Arabidopsis protein with prion behavior.Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomesPrions are a common mechanism for phenotypic inheritance in wild yeasts.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.The [Het-s] prion, an amyloid fold as a cell death activation triggerFitness landscape transformation through a single amino acid change in the rho terminator.Does the central dogma still stand?Defining the limits: Protein aggregation and toxicity in vivoProtein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB).Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.Pernicious pathogens or expedient elements of inheritance: the significance of yeast prions.The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity.Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation.High natural prevalence of a fungal prionNucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formationProkaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactionsSex, prions, and plasmids in yeast.Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)].Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.Aneuploidy causes proteotoxic stress in yeastCellular strategies for regulating functional and nonfunctional protein aggregation.
P2860
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P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Prions, protein homeostasis, and phenotypic diversity
@ast
Prions, protein homeostasis, and phenotypic diversity
@en
Prions, protein homeostasis, and phenotypic diversity
@nl
type
label
Prions, protein homeostasis, and phenotypic diversity
@ast
Prions, protein homeostasis, and phenotypic diversity
@en
Prions, protein homeostasis, and phenotypic diversity
@nl
prefLabel
Prions, protein homeostasis, and phenotypic diversity
@ast
Prions, protein homeostasis, and phenotypic diversity
@en
Prions, protein homeostasis, and phenotypic diversity
@nl
P2860
P1476
Prions, protein homeostasis, and phenotypic diversity
@en
P2093
Simon Alberti
P2860
P304
P356
10.1016/J.TCB.2009.12.003
P407
P577
2010-03-01T00:00:00Z