Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast.
about
Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentationSup35 methionine oxidation is a trigger for de novo [PSI(+)] prion formationThe [RNQ+] prion: a model of both functional and pathological amyloidHeritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Adaptive translation as a mechanism of stress response and adaptation.Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.One third of dynamic protein expression profiles can be predicted by a simple rate equation.Peroxiredoxins in plants and cyanobacteria.Protein expression regulation under oxidative stress.The ribosome-associated complex antagonizes prion formation in yeast.Prions in yeast.Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.Loss of vacuolar H+-ATPase (V-ATPase) activity in yeast generates an iron deprivation signal that is moderated by induction of the peroxiredoxin TSA2.Physiological and environmental control of yeast prions.Molecular targets of oxidative stress.Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stressHydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant.Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe.Autophagy protects against de novo formation of the [PSI+] prion in yeastExpression of salt-induced 2-Cys peroxiredoxin from Oryza sativa increases stress tolerance and fermentation capacity in genetically engineered yeast Saccharomyces cerevisiae.Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function.
P2860
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P2860
Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion 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
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@ast
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@en
type
label
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@ast
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@en
prefLabel
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@ast
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@en
P2093
P2860
P356
P1476
Ribosome-associated peroxiredo ...... of the [PSI+] prion in yeast.
@en
P2093
Chris M Grant
Klement Stojanovski
Mick F Tuite
Theodora C Sideri
P2860
P304
P356
10.1073/PNAS.1000347107
P407
P577
2010-03-22T00:00:00Z