Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.
about
Cofactor molecules maintain infectious conformation and restrict strain properties in purified prionsActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastHeritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].Prion formation and polyglutamine aggregation are controlled by two classes of genes.Curcumin prevents formation of polyglutamine aggregates by inhibiting Vps36, a component of the ESCRT-II complex.Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton.Heterologous aggregates promote de novo prion appearance via more than one mechanism.Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeletonLocalization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component.Modulation of efficiency of translation termination in Saccharomyces cerevisiae.An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiaePrions in yeast.Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.Study of amyloids using yeast[PSI(+) ] prion variant establishment in yeastExploring the basis of [PIN(+)] variant differences in [PSI(+)] inductionPhysiological and environmental control of yeast prions.Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.Analysis of [SWI+ ] formation and propagation events.A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity.Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.Toxicity and infectivity: insights from de novo prion formation.Autophagy protects against de novo formation of the [PSI+] prion in yeastHsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.
P2860
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P2860
Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.
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
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@ast
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@en
type
label
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@ast
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@en
prefLabel
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@ast
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@en
P2093
P2860
P356
P1476
Analyzing the birth and propag ...... SI+] and [Het-s](y), in yeast.
@en
P2093
Vibha Taneja
Vidhu Mathur
P2860
P304
P356
10.1091/MBC.E09-11-0927
P577
2010-03-10T00:00:00Z